Please use this identifier to cite or link to this item:
https://hdl.handle.net/10316/5273
Title: | Membrane domain formation by calcium-dependent, lipid-binding proteins: insights from the C2 motif | Authors: | Hinderliter, Anne K. Almeida, Paulo F. F. Biltonen, Rodney L. Creutz, Carl E. |
Keywords: | C2 motif; Annexin; Membrane domain; Ca2+- and lipid-binding proteins; Monte Carlo simulation; Pyrene fluorescence | Issue Date: | 1998 | Citation: | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1448:2 (1998) 227-235 | Abstract: | We propose a novel role in cellular function for some membrane-binding proteins and, specifically, the C2 motif. The C2 motif binds phospholipid in a manner that is modulated by Ca2+ and is thought to confer membrane-binding ability on a wide variety of proteins, primarily proteins involved in signal transduction and membrane trafficking events. We hypothesize that in the absence of Ca2+ the C2 motif couples the free energy of binding to a bilayer membrane comprised of zwitterionic and negatively charged lipids to the formation of a domain enriched in the negative lipids. This in turn leads to the dynamic clustering of bound homologous or heterologous proteins incorporating the C2 motif, or other acidic lipid-binding motifs. In the presence of Ca2+, the protein clusters may be further stabilized. In support of this hypothesis we present evidence for membrane domain formation by the first C2 domain of synaptotagmin in the absence of Ca2+. Fluid state phospholipid mixtures incorporating a pyrene-labeled phospholipid probe exhibited a change in pyrene excimer/monomer fluorescence ratio consistent with domain formation upon binding the C2 domain. In addition, we present the results of simulations of the interaction of the C2 domain with the membrane that indicate that protein clusters and lipid domains form in concert. | URI: | https://hdl.handle.net/10316/5273 | DOI: | 10.1016/S0167-4889(98)00146-3 | Rights: | openAccess |
Appears in Collections: | FCTUC Química - Artigos em Revistas Internacionais |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
file709b2a1d77e24c00847ed533fc61f760.pdf | 205.27 kB | Adobe PDF | View/Open |
SCOPUSTM
Citations
24
checked on Oct 14, 2024
WEB OF SCIENCETM
Citations
23
checked on Oct 2, 2024
Page view(s) 50
414
checked on Oct 15, 2024
Download(s)
333
checked on Oct 15, 2024
Google ScholarTM
Check
Altmetric
Altmetric
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.