Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins.

Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins. Research Abstract Details 

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Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins. Abstract Text:

Jeffrey R Kuhn,Thomas D Pollard,

We investigated how heterodimeric capping proteins bind to and dissociate from the barbed ends of actin filaments by observing single muscle actin filaments by total internal reflection fluorescence microscopy. The barbed end rate constants for mouse capping protein (CP) association of 2.6 x 10(6) M(-1) s(-1) and dissociation of 0.0003 s(-1) agree with published values measured in bulk assays. The polyphosphoinositides (PPIs), phosphatidylinositol 3,4-bisphosphate (PI(3,4)P(2)), PI(4,5)P(2), and PI(3,4,5)P(3), prevent CP from binding to barbed ends, but three different assays showed that none of these lipids dissociate CP from filaments at concentrations that block CP binding to barbed ends. The affinity of fission yeast CP for barbed ends is a thousandfold less than mouse CP, because of a slower association rate constant (1.1 x 10(5) M(-1) s(-1)) and a faster dissociation rate constant (0.004 s(-1)). PPIs do not inhibit binding of fission yeast CP to filament ends. Comparison of homology models revealed that fission yeast CP lacks a large patch of basic residues along the actin-binding surface on mouse CP. PPIs binding to this site might interfere sterically with capping, but this site would be inaccessible when CP is bound to the end of a filament.

Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins. Publishing Authors By Initials

JR Kuhn,TD Pollard,

For similar fungi: ascomycota: schizosaccharomyces research abstracts see: fungi: ascomycota: schizosaccharomyces research

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Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins. Journal Published:

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

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 28014-24

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 26

MONTH: 07

YEAR: 2007

Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins. Information

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LANGUAGE: eng

NlmUniqueID: 2985121

Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins. Keywords Mesh Terms:

KEYWORDS: Schizosaccharomyces

MESH TERMS: metabolism

Chemical & Substance for Abstract: Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins. Information

Substance Name: Polymers

Registry Number: 0

Grant and Affiliation Information for Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins.

AFFILIATION: Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM-26338

ACRONYM: GM

MEDLINETA: J Biol Chem

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