光滑蛋白样1与原肌球蛋白和钙调蛋白的结合是相互排斥的，并受磷酸化调节。

Q2 Biochemistry, Genetics and Molecular Biology BMC Biochemistry Pub Date : 2017-03-21 DOI:10.1186/s12858-017-0080-6

Annegret Ulke-Lemée, David Hao Sun, Hiroaki Ishida, Hans J Vogel, Justin A MacDonald

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引用次数: 3

摘要

背景:平滑素样1蛋白(SMTNL1)可与原肌球蛋白(Tpm)和钙调蛋白(CaM)结合，这两种蛋白对平滑肌收缩过程至关重要。在平滑肌钙脱敏过程中，SMTNL1的Ser301位点被蛋白激酶A磷酸化，但SMTNL1磷酸化对Tpm和cam结合的影响尚未被研究。结果:通过Tpm- sepharose和CaM- sepharose的下拉研究，我们检测了Tpm结合、CaM结合、SMTNL1磷酸化和钙浓度之间的相互作用。磷酸化极大地增强了SMTNL1在体外与Tpm结合的能力;表面等离子体共振产生10倍的K - D值提高与磷酸化。对CaM结合的影响更为复杂，并随钙的可用性而变化。结论:CaM和Tpm与SMTNL1结合表明两者的结合是互斥的。

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Binding of smoothelin-like 1 to tropomyosin and calmodulin is mutually exclusive and regulated by phosphorylation.

Background: The smoothelin-like 1 protein (SMTNL1) can associate with tropomyosin (Tpm) and calmodulin (CaM), two proteins essential to the smooth muscle contractile process. SMTNL1 is phosphorylated at Ser301 by protein kinase A during calcium desensitization in smooth muscle, yet the effect of SMTNL1 phosphorylation on Tpm- and CaM-binding has yet to be investigated.

Results: Using pull down studies with Tpm-Sepharose and CaM-Sepharose, we examined the interplay between Tpm binding, CaM binding, phosphorylation of SMTNL1 and calcium concentration. Phosphorylation greatly enhanced the ability of SMTNL1 to associate with Tpm in vitro; surface plasmon resonance yielded a 10-fold enhancement in K _D value with phosphorylation. The effect on CaM binding is more complex and varies with the availability of calcium.

Conclusions: Combining both CaM and Tpm with SMTNL1 shows that the binding to both is mutually exclusive.

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来源期刊

BMC Biochemistry BIOCHEMISTRY & MOLECULAR BIOLOGY-

CiteScore

4.80

自引率

0.00%

发文量

审稿时长

3 months

期刊介绍： BMC Biochemistry is an open access journal publishing original peer-reviewed research articles in all aspects of biochemical processes, including the structure, function and dynamics of metabolic pathways, supramolecular complexes, enzymes, proteins, nucleic acids and small molecular components of organelles, cells and tissues. BMC Biochemistry (ISSN 1471-2091) is indexed/tracked/covered by PubMed, MEDLINE, BIOSIS, CAS, EMBASE, Scopus, Zoological Record, Thomson Reuters (ISI) and Google Scholar.