Binding of smoothelin-like 1 to tropomyosin and calmodulin is mutually exclusive and regulated by phosphorylation
| dc.contributor.author | Ulke-Lemée, Annegret | |
| dc.contributor.author | Sun, David H | |
| dc.contributor.author | Ishida, Hiroaki | |
| dc.contributor.author | Vogel, Hans J | |
| dc.contributor.author | MacDonald, Justin A | |
| dc.date.accessioned | 2018-09-26T12:00:43Z | |
| dc.date.available | 2018-09-26T12:00:43Z | |
| dc.date.issued | 2017-03-21 | |
| dc.date.updated | 2018-09-26T12:00:43Z | |
| dc.description.abstract | Abstract 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. | |
| dc.identifier.citation | BMC Biochemistry. 2017 Mar 21;18(1):5 | |
| dc.identifier.doi | https://doi.org/10.1186/s12858-017-0080-6 | |
| dc.identifier.uri | http://hdl.handle.net/1880/107863 | |
| dc.language.rfc3066 | en | |
| dc.rights.holder | The Author(s). | |
| dc.title | Binding of smoothelin-like 1 to tropomyosin and calmodulin is mutually exclusive and regulated by phosphorylation | |
| dc.type | Journal Article |