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Cited by 469

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

The Actin-Binding Protein Profilin Binds to PIP 2 and Inhibits Its Hydrolysis by Phospholipase C

Goldschmidt-Clermont, Pascal J., Machesky, Laura M., Baldassare, Joseph J., Pollard, Thomas D.·1990·Science
DOI 10.1126/science.2157283
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Abstract

Profilin is generally thought to regulate actin polymerization, but the observation that acidic phospholipids dissociate the complex of profilin and actin raised the possibility that profilin might also regulate lipid metabolism. Profilin isolated from platelets binds with high affinity to small clusters of phosphatidylinositol 4,5-bisphosphate (PIP 2 ) molecules in micelles and also in bilayers with other phospholipids. The molar ratio of the complex of profilin with PIP 2 is 1:7 in micelles of pure PIP 2 and 1:5 in bilayers composed largely of other phospholipids. Profilin competes efficiently with platelet cytosolic phosphoinositide-specific phospholipase C for interaction with the PIP 2 substrate and thereby inhibits PIP 2 hydrolysis by this enzyme. The cellular concentrations and binding characteristics of these molecules are consistent with profilin being a negative regulator of the phosphoinositide signaling pathway in addition to its established function as an inhibitor of actin polymerization.

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Research works printed but not linked: 48

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Cited by

Metadata

Authors
Goldschmidt-Clermont, P. J., Machesky, L. M., Baldassare, J. J., & Pollard, T. D.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
1990-03-30
Volume
247
Issue
4950
Pages
1575-1578
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.2157283
OpenAlex
W2078835916
Cited by
469
References
1
FWCI
19.04
Type
journal article
Language
en
Open access
closed

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