Pub Date : 2019-01-01DOI: 10.1177/2515256419838719
Hana Kimura, Kohei Arasaki, Moe Iitsuka, M. Tagaya
During lipid droplet (LD) formation, several key enzymes for neutral lipid biosynthesis, such as acyl-CoA synthetase 3 (ACSL3), translocate from the bilayer of the endoplasmic reticulum membrane or mitochondria-associated membrane to the monolayer surface of LDs. It has been recently shown that syntaxin 17 (Stx17) in cooperation with synaptosomal-associated protein of 23 kDa (SNAP23) facilitates the translocation of ACSL3 from the endoplasmic reticulum/mitochondria-associated membrane to LDs. In this study, we investigated whether lipid microdomains enriched in cholesterol and sphingolipids are important for the formation of LDs and the interaction of Stx17 with ACSL3 and SNAP23. Cholesterol depletion and blockage of ceramide synthesis by chemicals inhibited oleic acid (OA)-induced LD biogenesis and decreased the interaction of Stx17 with ACSL3 and SNAP23, whereas blockage of ganglioside GD3 synthesis by sialyltransferase knockdown interfered with LD biogenesis by affecting the interaction of Stx17 with SNAP23 but not ACSL3. Consistent with the requirement of GD3 in LD biogenesis, Stx17 was found to associate with GD3-containing membranes upon OA loading. SNAP23 and a minor fraction of Stx17 were found to reside in detergent-resistant membranes (DRMs), whereas OA treatment caused redistribution of ACSL3 and Stx17 to DRMs. Importantly, the redistribution of ACSL3 to DRMs was abrogated upon depletion of Stx17 or SNAP23. Taken together, our results highlight the importance of lipid microdomains enriched in cholesterol and sphingolipids as a platform for the interaction of Stx17 with ACSL3 and SNAP23 in LD biogenesis.
{"title":"Syntaxin 17 Recruits ACSL3 to Lipid Microdomains in Lipid Droplet Biogenesis","authors":"Hana Kimura, Kohei Arasaki, Moe Iitsuka, M. Tagaya","doi":"10.1177/2515256419838719","DOIUrl":"https://doi.org/10.1177/2515256419838719","url":null,"abstract":"During lipid droplet (LD) formation, several key enzymes for neutral lipid biosynthesis, such as acyl-CoA synthetase 3 (ACSL3), translocate from the bilayer of the endoplasmic reticulum membrane or mitochondria-associated membrane to the monolayer surface of LDs. It has been recently shown that syntaxin 17 (Stx17) in cooperation with synaptosomal-associated protein of 23 kDa (SNAP23) facilitates the translocation of ACSL3 from the endoplasmic reticulum/mitochondria-associated membrane to LDs. In this study, we investigated whether lipid microdomains enriched in cholesterol and sphingolipids are important for the formation of LDs and the interaction of Stx17 with ACSL3 and SNAP23. Cholesterol depletion and blockage of ceramide synthesis by chemicals inhibited oleic acid (OA)-induced LD biogenesis and decreased the interaction of Stx17 with ACSL3 and SNAP23, whereas blockage of ganglioside GD3 synthesis by sialyltransferase knockdown interfered with LD biogenesis by affecting the interaction of Stx17 with SNAP23 but not ACSL3. Consistent with the requirement of GD3 in LD biogenesis, Stx17 was found to associate with GD3-containing membranes upon OA loading. SNAP23 and a minor fraction of Stx17 were found to reside in detergent-resistant membranes (DRMs), whereas OA treatment caused redistribution of ACSL3 and Stx17 to DRMs. Importantly, the redistribution of ACSL3 to DRMs was abrogated upon depletion of Stx17 or SNAP23. Taken together, our results highlight the importance of lipid microdomains enriched in cholesterol and sphingolipids as a platform for the interaction of Stx17 with ACSL3 and SNAP23 in LD biogenesis.","PeriodicalId":87951,"journal":{"name":"Contact","volume":"1 9 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2019-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82872807","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-01-01DOI: 10.1177/2515256419883136
J. Slee, T. Levine
The endoplasmic reticulum (ER), the most pervasive organelle, exchanges information and material with many other organelles, but the extent of its interorganelle connections and the proteins that form bridges are not well known. The integral ER membrane protein vesicle-associated membrane protein-associated protein (VAP) is found in multiple bridges, interacting with many proteins that contain a short linear motif consisting of “two phenylalanines in an acidic tract” (FFAT). The VAP-FFAT interaction is the most common mechanism by which cytoplasmic proteins, particularly interorganelle bridges, target the ER. Therefore, predicting new FFAT motifs may both find new individual peripheral ER proteins and identify new routes of communication involving the ER. Here, we searched for FFAT motifs across whole proteomes. The excess of eukaryotic proteins with FFAT motifs over background was ≥0.8%, suggesting that this is the minimum number of peripheral ER proteins. In yeast, where VAP was previously known to bind 4 proteins with FFAT motifs, a detailed analysis of a subset of proteins predicted 20 FFAT motifs. Extrapolating these findings to the whole proteome estimated the number of FFAT motifs in yeast at approximately 50 to 55 (0.9% of proteome). Among these previously unstudied FFAT motifs, most have known functions outside the ER, so could be involved in interorganelle communication. Many of these can target well-characterized membrane contact sites; however, some are in nucleoli and eisosomes, organelles previously unknown to have molecular bridges to the ER. We speculate that the nucleolar and eisosomal proteins with predicted motifs may function while bridging to the ER, indicating novel ER–nucleolus and ER–eisosome routes of interorganelle communication.
{"title":"Systematic Prediction of FFAT Motifs Across Eukaryote Proteomes Identifies Nucleolar and Eisosome Proteins With the Predicted Capacity to Form Bridges to the Endoplasmic Reticulum","authors":"J. Slee, T. Levine","doi":"10.1177/2515256419883136","DOIUrl":"https://doi.org/10.1177/2515256419883136","url":null,"abstract":"The endoplasmic reticulum (ER), the most pervasive organelle, exchanges information and material with many other organelles, but the extent of its interorganelle connections and the proteins that form bridges are not well known. The integral ER membrane protein vesicle-associated membrane protein-associated protein (VAP) is found in multiple bridges, interacting with many proteins that contain a short linear motif consisting of “two phenylalanines in an acidic tract” (FFAT). The VAP-FFAT interaction is the most common mechanism by which cytoplasmic proteins, particularly interorganelle bridges, target the ER. Therefore, predicting new FFAT motifs may both find new individual peripheral ER proteins and identify new routes of communication involving the ER. Here, we searched for FFAT motifs across whole proteomes. The excess of eukaryotic proteins with FFAT motifs over background was ≥0.8%, suggesting that this is the minimum number of peripheral ER proteins. In yeast, where VAP was previously known to bind 4 proteins with FFAT motifs, a detailed analysis of a subset of proteins predicted 20 FFAT motifs. Extrapolating these findings to the whole proteome estimated the number of FFAT motifs in yeast at approximately 50 to 55 (0.9% of proteome). Among these previously unstudied FFAT motifs, most have known functions outside the ER, so could be involved in interorganelle communication. Many of these can target well-characterized membrane contact sites; however, some are in nucleoli and eisosomes, organelles previously unknown to have molecular bridges to the ER. We speculate that the nucleolar and eisosomal proteins with predicted motifs may function while bridging to the ER, indicating novel ER–nucleolus and ER–eisosome routes of interorganelle communication.","PeriodicalId":87951,"journal":{"name":"Contact","volume":"PP 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2019-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84861313","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2018-11-27DOI: 10.1177/2515256418814621
Samantha K. Dziurdzik, Björn D. M. Bean, E. Conibear
Membrane contact sites are regulated through the controlled recruitment of constituent proteins. Yeast vacuolar protein sorting 13 (Vps13) dynamically localizes to membrane contact sites at endosomes, vacuoles, mitochondria, and the endoplasmic reticulum under different cellular conditions and is recruited to the prospore membrane during meiosis. Prior to our recent work, the mechanism for localization at contact sites was largely unknown. We identified Ypt35 as a novel Vps13 adaptor for endosomes and the nucleus-vacuole junction. Furthermore, we discovered a conserved recruitment motif in Ypt35 and found related motifs in the prospore membrane and mitochondrial adaptors, Spo71 and Mcp1, respectively. All three adaptors compete for binding to a six-repeat region of Vps13, suggesting adaptor competition regulates Vps13 localization. Here, we summarize and discuss the implications of our work, highlighting key outstanding questions.
{"title":"An Interorganellar Bidding War: Vps13 Localization by Competitive Organelle-Specific Adaptors","authors":"Samantha K. Dziurdzik, Björn D. M. Bean, E. Conibear","doi":"10.1177/2515256418814621","DOIUrl":"https://doi.org/10.1177/2515256418814621","url":null,"abstract":"Membrane contact sites are regulated through the controlled recruitment of constituent proteins. Yeast vacuolar protein sorting 13 (Vps13) dynamically localizes to membrane contact sites at endosomes, vacuoles, mitochondria, and the endoplasmic reticulum under different cellular conditions and is recruited to the prospore membrane during meiosis. Prior to our recent work, the mechanism for localization at contact sites was largely unknown. We identified Ypt35 as a novel Vps13 adaptor for endosomes and the nucleus-vacuole junction. Furthermore, we discovered a conserved recruitment motif in Ypt35 and found related motifs in the prospore membrane and mitochondrial adaptors, Spo71 and Mcp1, respectively. All three adaptors compete for binding to a six-repeat region of Vps13, suggesting adaptor competition regulates Vps13 localization. Here, we summarize and discuss the implications of our work, highlighting key outstanding questions.","PeriodicalId":87951,"journal":{"name":"Contact","volume":"25 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2018-11-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89428017","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2018-11-15DOI: 10.1177/2515256418809730
Thomas Di Mattia, C. Tomasetto, F. Alpy
Interorganelle membrane contact sites are subcellular structures that favor exchange and communication inside the cell. Such microdomains are built by molecular bridges that create a physical connection between two distinct organelles. The field of contact sites is now flourishing with discoveries of new tethering molecules. In that context, we identified by an unbiased proteomic approach a novel scaffold protein named MOtile SPerm Domain-containing protein 2 (MOSPD2). MOSPD2 is an endoplasmic reticulum (ER)-resident protein that is able to interact with several organelle-bound proteins that possess a small motif, named FFAT (two phenylalanines in an acidic tract). Consequently, we showed that MOSPD2 and its protein partners build contacts between the ER and endosomes, mitochondria, or Golgi. These findings highlight a new way for docking organelles on the ER.
{"title":"A Third Musketeer on the ER: MOSPD2 is a Novel VAP-related Receptor for FFAT Motifs","authors":"Thomas Di Mattia, C. Tomasetto, F. Alpy","doi":"10.1177/2515256418809730","DOIUrl":"https://doi.org/10.1177/2515256418809730","url":null,"abstract":"Interorganelle membrane contact sites are subcellular structures that favor exchange and communication inside the cell. Such microdomains are built by molecular bridges that create a physical connection between two distinct organelles. The field of contact sites is now flourishing with discoveries of new tethering molecules. In that context, we identified by an unbiased proteomic approach a novel scaffold protein named MOtile SPerm Domain-containing protein 2 (MOSPD2). MOSPD2 is an endoplasmic reticulum (ER)-resident protein that is able to interact with several organelle-bound proteins that possess a small motif, named FFAT (two phenylalanines in an acidic tract). Consequently, we showed that MOSPD2 and its protein partners build contacts between the ER and endosomes, mitochondria, or Golgi. These findings highlight a new way for docking organelles on the ER.","PeriodicalId":87951,"journal":{"name":"Contact","volume":"9 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2018-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76125168","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2018-06-11DOI: 10.1177/2515256418779685
A. Harada
Cholesterol is an essential component of membrane lipids and a starting material for hormone synthesis. After cholesterol is delivered to the cell as low-density lipoprotein, it is endocytosed and degraded in lysosomes to liberate free cholesterol. Free cholesterol is transported to the endoplasmic reticulum (ER) and esterified for further use. However, the mechanisms that transport cholesterol from lysosomes to the endoplasmic reticulum are poorly understood. We searched for binding proteins of a small GTP-binding protein, Rab11, and identified a novel protein, Rab11-binding protein containing LisH, coiled coil, and heat repeats (RELCH). RELCH also binds to oxysterol-binding protein (OSBP), an essential protein for nonvesicular cholesterol transport. The Rab11-RELCH-OSBP complex was found to tether to recycling endosomes and the trans-Golgi network, thereby mediating nonvesicular cholesterol transport between them. This pathway is distinct from the cholesterol transport pathway identified previously. In the absence of this complex, cholesterol accumulates in lysosomes in vitro and in vivo, suggesting the involvement of this complex in diseases associated with cholesterol transport.
{"title":"A Novel Contact by a Novel Protein Complex Supports Cholesterol Transport to the Endoplasmic Reticulum","authors":"A. Harada","doi":"10.1177/2515256418779685","DOIUrl":"https://doi.org/10.1177/2515256418779685","url":null,"abstract":"Cholesterol is an essential component of membrane lipids and a starting material for hormone synthesis. After cholesterol is delivered to the cell as low-density lipoprotein, it is endocytosed and degraded in lysosomes to liberate free cholesterol. Free cholesterol is transported to the endoplasmic reticulum (ER) and esterified for further use. However, the mechanisms that transport cholesterol from lysosomes to the endoplasmic reticulum are poorly understood. We searched for binding proteins of a small GTP-binding protein, Rab11, and identified a novel protein, Rab11-binding protein containing LisH, coiled coil, and heat repeats (RELCH). RELCH also binds to oxysterol-binding protein (OSBP), an essential protein for nonvesicular cholesterol transport. The Rab11-RELCH-OSBP complex was found to tether to recycling endosomes and the trans-Golgi network, thereby mediating nonvesicular cholesterol transport between them. This pathway is distinct from the cholesterol transport pathway identified previously. In the absence of this complex, cholesterol accumulates in lysosomes in vitro and in vivo, suggesting the involvement of this complex in diseases associated with cholesterol transport.","PeriodicalId":87951,"journal":{"name":"Contact","volume":"4 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2018-06-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81470664","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2018-05-10DOI: 10.1177/2515256418770512
A. V. van Vliet, M. Sassano, P. Agostinis
The endoplasmic reticulum (ER) is the most extensive organelle of the eukaryotic cell and constitutes the major site of protein and lipid synthesis and regulation of intracellular Ca2+ levels. To exert these functions properly, the ER network is shaped in structurally and functionally distinct domains that dynamically remodel in response to intrinsic and extrinsic cues. Moreover, the ER establishes a tight communication with virtually all organelles of the cell through specific subdomains called membrane contact sites. These contact sites allow preferential, nonvesicular channeling of key biological mediators including lipids and Ca2+ between organelles and are harnessed by the ER to interface with and coregulate a variety of organellar functions that are vital to maintain homeostasis. When ER homeostasis is lost, a condition that triggers the activation of an evolutionarily conserved pathway called the unfolded protein response (UPR), the ER undergoes rapid remodeling. These dynamic changes in ER morphology are functionally coupled to the modulation or formation of contact sites with key organelles, such as mitochondria and the plasma membrane, which critically regulate cell fate decisions of the ER-stressed cells. Certain components of the UPR have been shown to facilitate the formation of contact sites through various mechanisms including remodeling of the actin cytoskeleton. In this review, we discuss old and emerging evidence linking the UPR machinery to contact site formation in mammalian cells and discuss their important role in cellular homeostasis.
{"title":"The Unfolded Protein Response and Membrane Contact Sites: Tethering as a Matter of Life and Death?","authors":"A. V. van Vliet, M. Sassano, P. Agostinis","doi":"10.1177/2515256418770512","DOIUrl":"https://doi.org/10.1177/2515256418770512","url":null,"abstract":"The endoplasmic reticulum (ER) is the most extensive organelle of the eukaryotic cell and constitutes the major site of protein and lipid synthesis and regulation of intracellular Ca2+ levels. To exert these functions properly, the ER network is shaped in structurally and functionally distinct domains that dynamically remodel in response to intrinsic and extrinsic cues. Moreover, the ER establishes a tight communication with virtually all organelles of the cell through specific subdomains called membrane contact sites. These contact sites allow preferential, nonvesicular channeling of key biological mediators including lipids and Ca2+ between organelles and are harnessed by the ER to interface with and coregulate a variety of organellar functions that are vital to maintain homeostasis. When ER homeostasis is lost, a condition that triggers the activation of an evolutionarily conserved pathway called the unfolded protein response (UPR), the ER undergoes rapid remodeling. These dynamic changes in ER morphology are functionally coupled to the modulation or formation of contact sites with key organelles, such as mitochondria and the plasma membrane, which critically regulate cell fate decisions of the ER-stressed cells. Certain components of the UPR have been shown to facilitate the formation of contact sites through various mechanisms including remodeling of the actin cytoskeleton. In this review, we discuss old and emerging evidence linking the UPR machinery to contact site formation in mammalian cells and discuss their important role in cellular homeostasis.","PeriodicalId":87951,"journal":{"name":"Contact","volume":"22 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2018-05-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82650540","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2018-04-03DOI: 10.1177/2515256418756111
C. Raiborg
As part of a starvation response, lysosomes cluster perinuclearly. This facilitates fusion between lysosomes and autophagosomes and ensures activation of catabolic processes. When nutrients are abundant, lysosomes rather translocate to the cell periphery where they contribute to anabolic signaling. The mechanisms underlying nutrient-dependent lysosome positioning have been enigmatic. Now, several recent reports shed light on these mechanisms, and we are beginning to understand how the nutritional status can control and coordinate lysosome translocation pathways. Interestingly, several of the mechanisms that control lysosome positioning depend on membrane contact sites.
{"title":"How Nutrients Orchestrate Lysosome Positioning","authors":"C. Raiborg","doi":"10.1177/2515256418756111","DOIUrl":"https://doi.org/10.1177/2515256418756111","url":null,"abstract":"As part of a starvation response, lysosomes cluster perinuclearly. This facilitates fusion between lysosomes and autophagosomes and ensures activation of catabolic processes. When nutrients are abundant, lysosomes rather translocate to the cell periphery where they contribute to anabolic signaling. The mechanisms underlying nutrient-dependent lysosome positioning have been enigmatic. Now, several recent reports shed light on these mechanisms, and we are beginning to understand how the nutritional status can control and coordinate lysosome translocation pathways. Interestingly, several of the mechanisms that control lysosome positioning depend on membrane contact sites.","PeriodicalId":87951,"journal":{"name":"Contact","volume":"15 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2018-04-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87474183","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2018-01-01DOI: 10.1177/2515256418764043
Non Miyata, O. Kuge
Maintenance of the cardiolipin (CL) level largely depends on Ups1-Mdm35 complex-mediated intramitochondrial phosphatidic acid transfer. In addition, the presence of an alternative CL accumulation pathway has been suggested in the yeast Saccharomyces cerevisiae. This pathway is independent of the Ups1-Mdm35 complex and stimulated by loss of Ups2, which forms a complex with Mdm35 and mediates intramitochondrial transfer of phosphatidylserine for phosphatidylethanolamine synthesis. Recently, we found that the alternative CL accumulation pathway is enhanced by a lowered phosphatidylethanolamine level, not by loss of Ups2 per se, and depends on three mitochondrial inner membrane proteins, Fmp30, Mdm31, and Mdm32.
{"title":"Fmp30, Mdm31, and Mdm32 Function in Ups1-Independent Cardiolipin Accumulation Under Low Phosphatidylethanolamine Conditions","authors":"Non Miyata, O. Kuge","doi":"10.1177/2515256418764043","DOIUrl":"https://doi.org/10.1177/2515256418764043","url":null,"abstract":"Maintenance of the cardiolipin (CL) level largely depends on Ups1-Mdm35 complex-mediated intramitochondrial phosphatidic acid transfer. In addition, the presence of an alternative CL accumulation pathway has been suggested in the yeast Saccharomyces cerevisiae. This pathway is independent of the Ups1-Mdm35 complex and stimulated by loss of Ups2, which forms a complex with Mdm35 and mediates intramitochondrial transfer of phosphatidylserine for phosphatidylethanolamine synthesis. Recently, we found that the alternative CL accumulation pathway is enhanced by a lowered phosphatidylethanolamine level, not by loss of Ups2 per se, and depends on three mitochondrial inner membrane proteins, Fmp30, Mdm31, and Mdm32.","PeriodicalId":87951,"journal":{"name":"Contact","volume":"7 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73634576","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2016-10-17DOI: 10.1515/9781474409094-005
{"title":"3 New dialect formation and time depth","authors":"","doi":"10.1515/9781474409094-005","DOIUrl":"https://doi.org/10.1515/9781474409094-005","url":null,"abstract":"","PeriodicalId":87951,"journal":{"name":"Contact","volume":"48 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2016-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82004537","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2016-10-17DOI: 10.1515/9781474409094-006
{"title":"4 Linguistic contact and near-relative relationships","authors":"","doi":"10.1515/9781474409094-006","DOIUrl":"https://doi.org/10.1515/9781474409094-006","url":null,"abstract":"","PeriodicalId":87951,"journal":{"name":"Contact","volume":"6 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2016-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82495894","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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