Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity.

Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity. Research Abstract Details 

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Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity. Abstract Text:

Miljan Simonovic,Zhushan Zhang,Carol D Cianci,Thomas A Steitz,Jon S Morrow,

AlphaII-spectrin is a major cortical cytoskeletal protein contributing to membrane organization and integrity. The Ca2+-activated binding of calmodulin to an unstructured insert in the 11th repeat unit of alphaII-spectrin enhances the susceptibility of spectrin to calpain cleavage but abolishes its sensitivity to several caspases and to at least one bacterially derived pathologic protease. Other regulatory inputs including phosphorylation by c-Src also modulate the proteolytic susceptibility of alphaII-spectrin. These pathways, acting through spectrin, appear to control membrane plasticity and integrity in several cell types. To provide a structural basis for understanding these crucial biological events, we have solved the crystal structure of a complex between bovine calmodulin and the calmodulin-binding domain of human alphaII-spectrin (Protein Data Bank ID code 2FOT). The structure revealed that the entire calmodulin-spectrin-binding interface is hydrophobic in nature. The spectrin domain is also unique in folding into an amphiphilic helix once positioned within the calmodulin-binding groove. The structure of this complex provides insight into the mechanisms by which calmodulin, calpain, caspase, and tyrosine phosphorylation act on spectrin to regulate essential cellular processes.

Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity. Publishing Authors By Initials

M Simonovic,Z Zhang,CD Cianci,TA Steitz,JS Morrow,

For similar proteins: blood proteins: spectrin research abstracts see: proteins: blood proteins: spectrin research

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Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity. Journal Published:

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

Journal: The Journal of biological chemistry

VOLUME: 281

Page Numbers: 34333-40

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 31

MONTH: 08

YEAR: 2006

Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity. Keywords Mesh Terms:

KEYWORDS: Spectrin

MESH TERMS: metabolism

Chemical & Substance for Abstract: Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity. Information

Substance Name: Calpain

Registry Number: EC 3.4.22.-

Grant and Affiliation Information for Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity.

AFFILIATION: Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06520, USA.

Country: United States

AGENCY: United States NHLBI

GRANT: R01-HL28560

ACRONYM: HL

MEDLINETA: J Biol Chem

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