Annexin B12 is a sensor of membrane curvature and undergoes major curvature-dependent structural changes.

Annexin B12 is a sensor of membrane curvature and undergoes major curvature-dependent structural changes. Research Abstract Details 

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Annexin B12 is a sensor of membrane curvature and undergoes major curvature-dependent structural changes. Abstract Text:

Torsten Fischer,Lucy Lu,Harry T Haigler,Ralf Langen,

The regulation of membrane curvature plays an important role in many membrane trafficking and fusion events. Recent studies have begun to identify some of the proteins involved in controlling and sensing the curvature of cellular membranes. A mechanistic understanding of these processes is limited, however, as structural information for the membrane-bound forms of these proteins is scarce. Here, we employed a combination of biochemical and biophysical approaches to study the interaction of annexin B12 with membranes of different curvatures. We observed selective and Ca(2+)-independent binding of annexin B12 to negatively charged vesicles that were either highly curved or that contained lipids with negative intrinsic curvature. This novel curvature-dependent membrane interaction induced major structural rearrangements in the protein and resulted in a backbone fold that was different from that of the well characterized Ca(2+)-dependent membrane-bound form of annexin B12. Following curvature-dependent membrane interaction, the protein retained a predominantly alpha-helical structure but EPR spectroscopy studies of nitroxide side chains placed at selected sites on annexin B12 showed that the protein underwent inside-out refolding that brought previously buried hydrophobic residues into contact with the membrane. These structural changes were reminiscent of those previously observed following Ca(2+)-independent interaction of annexins with membranes at mildly acidic pH, yet they occurred at neutral pH in the presence of curved membranes. The present data demonstrate that annexin B12 is a sensor of membrane curvature and that membrane curvature can trigger large scale conformational changes. We speculate that membrane curvature could be a physiological signal that induces the previously reported Ca(2+)-independent membrane interaction of annexins in vivo.

Annexin B12 is a sensor of membrane curvature and undergoes major curvature-dependent structural changes. Publishing Authors By Initials

T Fischer,L Lu,HT Haigler,R Langen,

For similar proteins: recombinant proteins research abstracts see: proteins: recombinant proteins research

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Annexin B12 is a sensor of membrane curvature and undergoes major curvature-dependent structural changes. Journal Published:

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

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 9996-10004

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 31

MONTH: 01

YEAR: 2007

Annexin B12 is a sensor of membrane curvature and undergoes major curvature-dependent structural changes. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Annexin B12 is a sensor of membrane curvature and undergoes major curvature-dependent structural changes. Keywords Mesh Terms:

KEYWORDS: Recombinant Proteins

MESH TERMS: chemistry

Chemical & Substance for Abstract: Annexin B12 is a sensor of membrane curvature and undergoes major curvature-dependent structural changes. Information

Substance Name: Recombinant Proteins

Registry Number: 0

Grant and Affiliation Information for Annexin B12 is a sensor of membrane curvature and undergoes major curvature-dependent structural changes.

AFFILIATION: Department of Biochemistry and Molecular Biology, Keck School of Medicine, University of Southern California, Los Angeles, California 90033, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM 63915

ACRONYM: GM

MEDLINETA: J Biol Chem

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