Unphosphorylated twitchin forms a complex with actin and myosin that may contribute to tension maintenance in catch.

Unphosphorylated twitchin forms a complex with actin and myosin that may contribute to tension maintenance in catch. Research Abstract Details 

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Unphosphorylated twitchin forms a complex with actin and myosin that may contribute to tension maintenance in catch. Abstract Text:

Daisuke Funabara,Chieko Hamamoto,Koji Yamamoto,Akinori Inoue,Miki Ueda,Rika Osawa,Satoshi Kanoh,David J Hartshorne,Suechika Suzuki,Shugo Watabe,Daisuke Funabara,Chieko Hamamoto,Koji Yamamoto,Akinori Inoue,Miki Ueda,Rika Osawa,Satoshi Kanoh,David J Hartshorne,Suechika Suzuki,Shugo Watabe,

Molluscan smooth muscle can maintain tension over extended periods with little energy expenditure, a process termed catch. Catch is thought to be regulated by phosphorylation of a thick filament protein, twitchin, and involves two phosphorylation sites, D1 and D2, close to the N and C termini, respectively. This study was initiated to investigate the role of the D2 site and its phosphorylation in the catch mechanism. A peptide was constructed containing the D2 site and flanking immunoglobulin (Ig) motifs. It was shown that the dephosphorylated peptide, but not the phosphorylated form, bound to both actin and myosin. The binding site on actin was within the sequence L10 to P29. This region also binds to loop 2 of the myosin head. The dephosphorylated peptide linked myosin and F-actin and formed a trimeric complex. Electron microscopy revealed that twitchin is distributed on the surface of the thick filament with an axial periodicity of 36.25 nm and it is suggested that the D2 site aligns with the myosin heads. It is proposed that the complex formed with the dephosphorylated D2 site of twitchin, F-actin and myosin represents a component of the mechanical linkage in catch.

Unphosphorylated twitchin forms a complex with actin and myosin that may contribute to tension maintenance in catch. Publishing Authors By Initials

D Funabara,C Hamamoto,K Yamamoto,A Inoue,M Ueda,R Osawa,S Kanoh,DJ Hartshorne,S Suzuki,S Watabe,D Funabara,C Hamamoto,K Yamamoto,A Inoue,M Ueda,R Osawa,S Kanoh,DJ Hartshorne,S Suzuki,S Watabe,

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Unphosphorylated twitchin forms a complex with actin and myosin that may contribute to tension maintenance in catch. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of experimental biology

VOLUME: 210

Page Numbers: 4399-410

Journal Abbreviation: J. Exp. Biol.

ISSN: 0022-0949

DAY: 6

MONTH: Dec

YEAR: 2007

Unphosphorylated twitchin forms a complex with actin and myosin that may contribute to tension maintenance in catch. Information

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LANGUAGE: eng

NlmUniqueID: 243705

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Grant and Affiliation Information for Unphosphorylated twitchin forms a complex with actin and myosin that may contribute to tension maintenance in catch.

AFFILIATION: Graduate School of Bioresources, Mie University, Tsu, Mie 514-8507, Japan.

Country: England

AGENCY: United States NHLBI

GRANT: HL 23615

ACRONYM: HL

MEDLINETA: J Exp Biol

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