Binding of myotrophin/V-1 to actin-capping protein: implications for how capping protein binds to the filament barbed end.

Binding of myotrophin/V-1 to actin-capping protein: implications for how capping protein binds to the filament barbed end. Research Abstract Details 

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Binding of myotrophin/V-1 to actin-capping protein: implications for how capping protein binds to the filament barbed end. Abstract Text:

Nandini Bhattacharya,Shatadal Ghosh,David Sept,John A Cooper,Nandini Bhattacharya,Shatadal Ghosh,David Sept,John A Cooper,

The heterodimeric actin-capping protein (CP) regulates actin assembly and cell motility by binding tightly to the barbed end of the actin filament. Here we demonstrate that myotrophin/V-1 binds directly to CP in a 1:1 molar ratio with a Kd of 10-50 nm. V-1 binding inhibited the ability of CP to cap the barbed ends of actin filaments. The actin-binding COOH-terminal region, the "tentacle," of the CP beta subunit was important for binding V-1, with lesser contributions from the alpha subunit COOH-terminal region and the body of the protein. V-1 appears to be unable to bind to CP that is on the barbed end, based on the observations that V-1 had no activity in an uncapping assay and that the V-1.CP complex had no capping activity. Two loops of V-1, which extend out from the alpha-helical backbone of this ankyrin repeat protein, were necessary for V-1 to bind CP. Parallel computational studies determined a bound conformation of the beta tentacle with V-1 that is consistent with these findings, and they offered insight into experimentally observed differences between the alpha1 and alpha2 isoforms as well as the mutant lacking the alpha tentacle. These results support and extend our "wobble" model for CP binding to the actin filament, in which the two COOH-terminal regions of CP bind independently to the actin filament, and bound CP is able to wobble when attached only via its mobile beta-subunit tentacle. This model is also supported by molecular dynamics simulations of CP reported here. The existence of the wobble state may be important for actin dynamics in cells.

Binding of myotrophin/V-1 to actin-capping protein: implications for how capping protein binds to the filament barbed end. Publishing Authors By Initials

N Bhattacharya,S Ghosh,D Sept,JA Cooper,N Bhattacharya,S Ghosh,D Sept,JA Cooper,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research

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Binding of myotrophin/V-1 to actin-capping protein: implications for how capping protein binds to the filament barbed end. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: The Journal of biological chemistry

VOLUME: 281

Page Numbers: 31021-30

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 7

MONTH: 08

YEAR: 2006

Binding of myotrophin/V-1 to actin-capping protein: implications for how capping protein binds to the filament barbed end. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Binding of myotrophin/V-1 to actin-capping protein: implications for how capping protein binds to the filament barbed end. Keywords Mesh Terms:

KEYWORDS: Structure-Activity Relationship

MESH TERMS: chemistry

Chemical & Substance for Abstract: Binding of myotrophin/V-1 to actin-capping protein: implications for how capping protein binds to the filament barbed end. Information

Substance Name: myotrophin

Registry Number: 0

Grant and Affiliation Information for Binding of myotrophin/V-1 to actin-capping protein: implications for how capping protein binds to the filament barbed end.

AFFILIATION: Department of Cell Biology and Physiology, Washington University, St. Louis, Missouri 63110, USA.

Country: United States

AGENCY: United States NHLBI

GRANT: T32 HL007873

ACRONYM: HL

MEDLINETA: J Biol Chem

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