Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
Volume 1761, Issue 8, Pages 805-811Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbalip.2006.02.020
Keywords
protein kinase C; diacylglycerol; phosphoinositide; signal transduction; membrane trafficking
Funding
- Intramural NIH HHS [Z01 DK036118-14] Funding Source: Medline
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Eukaryotic signaling and trafficking proteins are rich in modular domains that bind cell membranes. These binding events are tightly regulated in space and time. The structural, biochemical, and biophysical mechanisms for targeting have been worked out for many families of membrane binding domains. This review takes a comparative view of seven major classes of membrane binding domains, the C1, C2, PH, FYVE, PX, ENTH, and BAR domains. These domains use a combination of specific headgroup interactions, hydrophobic membrane penetration, electrostatic surface interactions, and shape complementarity to bind to specific subcellular membranes. Published by Elsevier B.V.
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