Journal
PHYSICAL BIOLOGY
Volume 8, Issue 3, Pages -Publisher
IOP PUBLISHING LTD
DOI: 10.1088/1478-3975/8/3/035005
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Funding
- Japan Science and Technology Agency [ERATO, BIRD]
- Japan Society for the Promotion of Science [20227008, 21113007]
- Uehara Memorial Foundation
- Grants-in-Aid for Scientific Research [20227008, 21113007] Funding Source: KAKEN
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The actin capping protein (CP) tightly binds to the barbed end of actin filaments to block further elongation. The beta-tentacle in CP is an important region that ensures stable interaction with actin filaments. CARMIL inhibits the interaction of CP with actin filaments via the C-terminal portion containing the CP-binding motif, located in an intrinsically disordered region. We have proposed an allosteric inhibition model in which CARMIL suppresses CP by the population shift mechanism. Here, we solved a crystal structure of CP in complex with a CARMIL-derived peptide, CA32. The new structure clearly represents the a-helical form of the beta-tentacle that was invisible in other CP/CARMIL peptide complex structures. In addition, we exhaustively performed a normal mode analysis with the elastic network model on all available crystal structures of the CP/CARMIL peptide complexes, including the new structure. We concluded that the CP-binding motif is necessary and sufficient for altering the fluctuation of CP, which is essential for attenuating the barbed-end-capping activity along the population shift mechanism. The roles and functions of the beta-tentacle and the CP-binding motif are discussed in terms of their intrinsically disordered nature.
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