CaMKII in addition to MLCK contributes to phosphorylation of regulatory light chain in cardiomyocytes
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- 作者：Hilde Eikemoa ; b ; 1 ; hilde.eikemo@ntnu.no" class="auth_mail" title="E-mail the corresponding author ; Lise Romá ; n Moltzaua ; b ; 1 ; l.r.moltzau@medisin.uio.no" class="auth_mail" title="E-mail the corresponding author ; Rizwan I. Hussaina ; b ; rizwan.hussain@medisin.uio.no" class="auth_mail" title="E-mail the corresponding author ; Cam H.T. Nguyena ; b ; Eirik Qvigstada ; b ; eirik.qvigstad@medisin.uio.no" class="auth_mail" title="E-mail the corresponding author ; Finn Olav Levya ; b ; f.o.levy@medisin.uio.no" class="auth_mail" title="E-mail the corresponding author ; Tor Skomedala ; b ; tor.skomedal@medisin.uio.no" class="auth_mail" title="E-mail the corresponding author ; Jan-Bjø ; rn Osnesa ; b ; j.b.osnes@medisin.uio.no" class="auth_mail" title="E-mail the corresponding author
- 关键词：Regulatory light chain (RLC ; Myosin light chain 2 ; MLC2) ; Phosphorylation ; Myosin light chain kinase (MLCK) ; Ca2+/calmodulin-dependent kinase II (CaMKII) ; Phosphatase inhibition
- 刊名：Biochemical and Biophysical Research Communications
- 出版年：2016
- 出版时间：26 February 2016
- 年：2016
- 卷：471
- 期：1
- 页码：219-225
- 全文大小：913 K
文摘
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Phosphatase inhibition unmasks kinase activity.
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CaMKII in addition to MLCK phosphorylates RLC in cardiomyocytes.
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Involvement of other kinases than MLCK and CaMKII cannot be excluded.