Cardiac leiomodin2 binds to the sides of actin filaments and regulates the ATPase activity of myosin.
Cardiac leiomodin2 binds to the sides of actin filaments and regulates the ATPase activity of myosin.
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DOI：
10.1371/journal.pone.0186288
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发表时间：
2017
期刊：
影响因子：
3.7
通讯作者：
Nyitrai M
中科院分区：
文献类型：
--
作者：
Szatmári D;Bugyi B;Ujfalusi Z;Grama L;Dudás R;Nyitrai M
Leiomodin proteins are vertebrate homologues of tropomodulin, having a role in the assembly and maintenance of muscle thin filaments. Leiomodin2 contains an N-terminal tropomodulin homolog fragment including tropomyosin-, and actin-binding sites, and a C-terminal Wiskott-Aldrich syndrome homology 2 actin-binding domain. The cardiac leiomodin2 isoform associates to the pointed end of actin filaments, where it supports the lengthening of thin filaments and competes with tropomodulin. It was recently found that cardiac leiomodin2 can localise also along the length of sarcomeric actin filaments. While the activities of leiomodin2 related to pointed end binding are relatively well described, the potential side binding activity and its functional consequences are less well understood. To better understand the biological functions of leiomodin2, in the present work we analysed the structural features and the activities of Rattus norvegicus cardiac leiomodin2 in actin dynamics by spectroscopic and high-speed sedimentation approaches. By monitoring the fluorescence parameters of leiomodin2 tryptophan residues we found that it possesses flexible, intrinsically disordered regions. Leiomodin2 accelerates the polymerisation of actin in an ionic strength dependent manner, which relies on its N-terminal regions. Importantly, we demonstrate that leiomodin2 binds to the sides of actin filaments and induces structural alterations in actin filaments. Upon its interaction with the filaments leiomodin2 decreases the actin-activated Mg2+-ATPase activity of skeletal muscle myosin. These observations suggest that through its binding to side of actin filaments and its effect on myosin activity leiomodin2 has more functions in muscle cells than it was indicated in previous studies.
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影响因子：
16.6
作者：
Boczkowska M;Rebowski G;Kremneva E;Lappalainen P;Dominguez R
通讯作者：
Dominguez R
影响因子：
6.8
作者：
Dunker, A. Keith;Silman, Israel;Sussman, Joel L.
通讯作者：
Sussman, Joel L.
影响因子：
15.9
作者：
Cenik, Bercin K.;Garg, Ankit;Liu, Ning
通讯作者：
Liu, Ning
DOI：
10.1152/ajpcell.2001.280.6.c1645
发表时间：
2001-06-01
影响因子：
5.5
作者：
Conley, CA
通讯作者：
Conley, CA
影响因子：
2.7
作者：
HIGUCHI, H;TAKEMORI, S
通讯作者：
TAKEMORI, S