{"title":"Interactions between sea lice and their hosts.","authors":"Stewart C Johnson, Mark D Fast","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":22134,"journal":{"name":"Symposia of the Society for Experimental Biology","volume":" 55","pages":"131-59; discussion 243-5"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24753585","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}
Philippe Collas, Sandra B Martins, Helga B Landsverk
The cell nucleus is a highly dynamic organelle whose function and structure during the cell cycle is tightly controlled. A number of signals triggered by external stimuli or intracellular clocks are relayed to the nucleus by protein kinases and phosphatases. Specificity of action of kinases and phosphatases can be achieved by their recruitment into multiprotein complexes targeted to discrete subcellular or subnuclear loci. One class of molecules targeting signalling units within single complexes are A-kinase anchoring proteins or AKAPs. AKAPs not only target enzymes to their substrate but may also regulate enzyme activity. This chapter highlights the role of nuclear AKAPs in relaying and modulating protein kinase and phosphatase signals to the nucleus or chromosomes.
{"title":"Signalling to the nucleus via A-kinase anchoring proteins.","authors":"Philippe Collas, Sandra B Martins, Helga B Landsverk","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The cell nucleus is a highly dynamic organelle whose function and structure during the cell cycle is tightly controlled. A number of signals triggered by external stimuli or intracellular clocks are relayed to the nucleus by protein kinases and phosphatases. Specificity of action of kinases and phosphatases can be achieved by their recruitment into multiprotein complexes targeted to discrete subcellular or subnuclear loci. One class of molecules targeting signalling units within single complexes are A-kinase anchoring proteins or AKAPs. AKAPs not only target enzymes to their substrate but may also regulate enzyme activity. This chapter highlights the role of nuclear AKAPs in relaying and modulating protein kinase and phosphatase signals to the nucleus or chromosomes.</p>","PeriodicalId":22134,"journal":{"name":"Symposia of the Society for Experimental Biology","volume":" 56","pages":"245-63"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24831500","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 : 2004-01-01DOI: 10.4324/9780203643396-19
P. Clarke, Chuanmao Zhang
Using evidence derived primarily from studies using Xenopus egg extracts, a model for the role of Ran in multiple stages during NE assembly can be proposed (Figure 2). Ran is concentrated on chromatin prior to NE assembly and recruits RCC1 that generates Ran-GTP locally. Recruitment of RCC1 to chromatin may be a specialized mechanism to initiate NE assembly following fertilization of the egg, whereas in somatic cells, RCC1 may be present on chromatin throughout mitosis. Ran-GTP recruits vesicles to the surface of chromatin, and promotes vesicle fusion to form the double membrane of the NE. Ran-GTP may recruit membrane vesicles to chromatin through binding to integral membrane proteins through importin-beta. A transient complex would be formed between Ran-GTP, importin-beta and the target protein, which would be released locally to promote assembly of a precursor complex. GTP hydrolysis by Ran would release importin-beta, but may also play a role in vesicle fusion. Ran-GTP also promotes NPC assembly by releasing nucleoporins such as Nup107 from inhibitory complexes with importin-beta. In vertebrate cells undergoing mitosis, the majority of Ran molecules are excluded from the chromosomes and dispersed into the cytoplasm. Relocalization of Ran to chromatin at the end of mitosis may co-ordinate the initiation of NE assembly with disassembly of the mitotic spindle. The function of Ran in this transition is likely to be coupled to changes in the activity of cyclin-dependent protein kinases and other activities that control the progression of the cell cycle. Thus, changes in the localization of Ran and its regulators provide temporal and spatial control of NE assembly at the end of mitosis.
{"title":"Spatial and temporal control of nuclear envelope assembly by Ran GTPase.","authors":"P. Clarke, Chuanmao Zhang","doi":"10.4324/9780203643396-19","DOIUrl":"https://doi.org/10.4324/9780203643396-19","url":null,"abstract":"Using evidence derived primarily from studies using Xenopus egg extracts, a model for the role of Ran in multiple stages during NE assembly can be proposed (Figure 2). Ran is concentrated on chromatin prior to NE assembly and recruits RCC1 that generates Ran-GTP locally. Recruitment of RCC1 to chromatin may be a specialized mechanism to initiate NE assembly following fertilization of the egg, whereas in somatic cells, RCC1 may be present on chromatin throughout mitosis. Ran-GTP recruits vesicles to the surface of chromatin, and promotes vesicle fusion to form the double membrane of the NE. Ran-GTP may recruit membrane vesicles to chromatin through binding to integral membrane proteins through importin-beta. A transient complex would be formed between Ran-GTP, importin-beta and the target protein, which would be released locally to promote assembly of a precursor complex. GTP hydrolysis by Ran would release importin-beta, but may also play a role in vesicle fusion. Ran-GTP also promotes NPC assembly by releasing nucleoporins such as Nup107 from inhibitory complexes with importin-beta. In vertebrate cells undergoing mitosis, the majority of Ran molecules are excluded from the chromosomes and dispersed into the cytoplasm. Relocalization of Ran to chromatin at the end of mitosis may co-ordinate the initiation of NE assembly with disassembly of the mitotic spindle. The function of Ran in this transition is likely to be coupled to changes in the activity of cyclin-dependent protein kinases and other activities that control the progression of the cell cycle. Thus, changes in the localization of Ran and its regulators provide temporal and spatial control of NE assembly at the end of mitosis.","PeriodicalId":22134,"journal":{"name":"Symposia of the Society for Experimental Biology","volume":"5 1","pages":"193-204"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81327495","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}
It is clear that the roles of apoptosis in the interactions between the parasite and their non-mammalian hosts are multifaceted and highly dependent on individual associations between the two organisms involved. Whilst there are instances where both organisms appear to gain from the apoptotic mechanism induced, in the majority of cases apoptosis appears to favour only one of the parties. In the instances when the parasite benefits, the apoptosis has been related to infectivity and virulence, an interruption of the killing mechanism of the host, and liberation of the pathogen. However, there are occasions where the apoptotic process benefits the host, as controlled cell death has been associated with limiting the pathogen population, parasite migration within the host and, in some instances, actually killing the invading organism. Apoptosis thus appears to play several fundamental roles within the host-parasite relationship which is ultimately reflected in an effect on the host population either mediated through an alteration in host fecundity or reduction in host numbers. The next decade promises to be both exciting and productive with respect to our knowledge of the relationship between apoptosis in non-mammalian animals and infection. Over the last few years the information obtained from studies on the apoptotic process in mammals and invertebrates (i.e. C. elegans and Drosophila) have been effectively used to increase our understanding of the apoptotic process in other animals such as insects, fish and amphibians. Such knowledge has paved the way for extensive studies on the effect of infections to be carried out.
{"title":"The role of apoptosis in non-mammalian host-parasite relationships.","authors":"D. Hoole, Gwyn T. Williams","doi":"10.4324/9780203487709-2","DOIUrl":"https://doi.org/10.4324/9780203487709-2","url":null,"abstract":"It is clear that the roles of apoptosis in the interactions between the parasite and their non-mammalian hosts are multifaceted and highly dependent on individual associations between the two organisms involved. Whilst there are instances where both organisms appear to gain from the apoptotic mechanism induced, in the majority of cases apoptosis appears to favour only one of the parties. In the instances when the parasite benefits, the apoptosis has been related to infectivity and virulence, an interruption of the killing mechanism of the host, and liberation of the pathogen. However, there are occasions where the apoptotic process benefits the host, as controlled cell death has been associated with limiting the pathogen population, parasite migration within the host and, in some instances, actually killing the invading organism. Apoptosis thus appears to play several fundamental roles within the host-parasite relationship which is ultimately reflected in an effect on the host population either mediated through an alteration in host fecundity or reduction in host numbers. The next decade promises to be both exciting and productive with respect to our knowledge of the relationship between apoptosis in non-mammalian animals and infection. Over the last few years the information obtained from studies on the apoptotic process in mammals and invertebrates (i.e. C. elegans and Drosophila) have been effectively used to increase our understanding of the apoptotic process in other animals such as insects, fish and amphibians. Such knowledge has paved the way for extensive studies on the effect of infections to be carried out.","PeriodicalId":22134,"journal":{"name":"Symposia of the Society for Experimental Biology","volume":"8 1","pages":"13-44; discussion 243-5"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75164779","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}
Using evidence derived primarily from studies using Xenopus egg extracts, a model for the role of Ran in multiple stages during NE assembly can be proposed (Figure 2). Ran is concentrated on chromatin prior to NE assembly and recruits RCC1 that generates Ran-GTP locally. Recruitment of RCC1 to chromatin may be a specialized mechanism to initiate NE assembly following fertilization of the egg, whereas in somatic cells, RCC1 may be present on chromatin throughout mitosis. Ran-GTP recruits vesicles to the surface of chromatin, and promotes vesicle fusion to form the double membrane of the NE. Ran-GTP may recruit membrane vesicles to chromatin through binding to integral membrane proteins through importin-beta. A transient complex would be formed between Ran-GTP, importin-beta and the target protein, which would be released locally to promote assembly of a precursor complex. GTP hydrolysis by Ran would release importin-beta, but may also play a role in vesicle fusion. Ran-GTP also promotes NPC assembly by releasing nucleoporins such as Nup107 from inhibitory complexes with importin-beta. In vertebrate cells undergoing mitosis, the majority of Ran molecules are excluded from the chromosomes and dispersed into the cytoplasm. Relocalization of Ran to chromatin at the end of mitosis may co-ordinate the initiation of NE assembly with disassembly of the mitotic spindle. The function of Ran in this transition is likely to be coupled to changes in the activity of cyclin-dependent protein kinases and other activities that control the progression of the cell cycle. Thus, changes in the localization of Ran and its regulators provide temporal and spatial control of NE assembly at the end of mitosis.
{"title":"Spatial and temporal control of nuclear envelope assembly by Ran GTPase.","authors":"Paul R Clarke, Chuanmao Zhang","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Using evidence derived primarily from studies using Xenopus egg extracts, a model for the role of Ran in multiple stages during NE assembly can be proposed (Figure 2). Ran is concentrated on chromatin prior to NE assembly and recruits RCC1 that generates Ran-GTP locally. Recruitment of RCC1 to chromatin may be a specialized mechanism to initiate NE assembly following fertilization of the egg, whereas in somatic cells, RCC1 may be present on chromatin throughout mitosis. Ran-GTP recruits vesicles to the surface of chromatin, and promotes vesicle fusion to form the double membrane of the NE. Ran-GTP may recruit membrane vesicles to chromatin through binding to integral membrane proteins through importin-beta. A transient complex would be formed between Ran-GTP, importin-beta and the target protein, which would be released locally to promote assembly of a precursor complex. GTP hydrolysis by Ran would release importin-beta, but may also play a role in vesicle fusion. Ran-GTP also promotes NPC assembly by releasing nucleoporins such as Nup107 from inhibitory complexes with importin-beta. In vertebrate cells undergoing mitosis, the majority of Ran molecules are excluded from the chromosomes and dispersed into the cytoplasm. Relocalization of Ran to chromatin at the end of mitosis may co-ordinate the initiation of NE assembly with disassembly of the mitotic spindle. The function of Ran in this transition is likely to be coupled to changes in the activity of cyclin-dependent protein kinases and other activities that control the progression of the cell cycle. Thus, changes in the localization of Ran and its regulators provide temporal and spatial control of NE assembly at the end of mitosis.</p>","PeriodicalId":22134,"journal":{"name":"Symposia of the Society for Experimental Biology","volume":" 56","pages":"193-204"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24831496","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}
{"title":"Interactions between sea lice and their hosts.","authors":"Stewart C Johnson, M. Fast","doi":"10.4324/9780203487709-7","DOIUrl":"https://doi.org/10.4324/9780203487709-7","url":null,"abstract":"","PeriodicalId":22134,"journal":{"name":"Symposia of the Society for Experimental Biology","volume":"29 1","pages":"131-59; discussion 243-5"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72674015","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}
{"title":"Interactive associations between fish hosts and monogeneans.","authors":"K. Buchmann, T. Lindenstrøm, J. Bresciani","doi":"10.4324/9780203487709-8","DOIUrl":"https://doi.org/10.4324/9780203487709-8","url":null,"abstract":"","PeriodicalId":22134,"journal":{"name":"Symposia of the Society for Experimental Biology","volume":"43 1","pages":"161-84; discussion 243-5"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75142062","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}
{"title":"The nuclear envelope proteome.","authors":"Mathias Dreger, Henning Otto","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":22134,"journal":{"name":"Symposia of the Society for Experimental Biology","volume":" 56","pages":"9-40"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24830961","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}
M. E. Nielsen, T. Lindenstrøm, J. Sigh, K. Buchmann
{"title":"Thionine-positive cells in relation to parasites.","authors":"M. E. Nielsen, T. Lindenstrøm, J. Sigh, K. Buchmann","doi":"10.4324/9780203487709-3","DOIUrl":"https://doi.org/10.4324/9780203487709-3","url":null,"abstract":"","PeriodicalId":22134,"journal":{"name":"Symposia of the Society for Experimental Biology","volume":"142 1","pages":"45-66; discussion 243-5"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77329563","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}
M. Joerink, J. Saeij, J. Stafford, M. Belosevic, G. Wiegertjes
{"title":"Animal models for the study of innate immunity: protozoan infections in fish.","authors":"M. Joerink, J. Saeij, J. Stafford, M. Belosevic, G. Wiegertjes","doi":"10.4324/9780203487709-4","DOIUrl":"https://doi.org/10.4324/9780203487709-4","url":null,"abstract":"","PeriodicalId":22134,"journal":{"name":"Symposia of the Society for Experimental Biology","volume":"1 1","pages":"67-89; discussion 243-5"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77945943","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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