Pleckstrin
Pleckstrin-1 | |||||||
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Chr. 2 p13.3 | |||||||
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Chr. 14 q23.3q24.1 | |||||||
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Wikidata | Q18038260 | ||||||
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Pleckstrins are a family of
The pleckstrin homology domain (PH domain) was named after pleckstrin-1.[2]
Sequence and structure
Both pleckstrin-1 and pleckstrin-2 contain two pleckstrin homology domains, separated by a central dishevelled-Egl10-pleckstrin (DEP) domain. Pleckstrin-1 is phosphorylated by protein kinase C on three serine and threonine residues located between the first pleckstrin homology domain and the DEP domain;[2] pleckstrin-2 is not a substrate for protein kinase C.[2][4] The two proteins share 65% sequence homology [2] and have a size of about 47 kilodaltons.[5]
As of 2024, no high-resolution three-dimensional structure has been solved for full-length pleckstrin, but the structures of the individual domains of both pleckstrin-1 and -2 have been published.[2]
Functions
Pleckstrins are involved in rearranging the
Pleckstrin-1 is a key protein in the membrane remodelling processes that occur during platelet activation.
Pleckstrin-2 has roles in cell spreading, inflammation, erythropoeisis, and tumorigenesis. In lymphocytes, it is involved in
References
External links
- pleckstrin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)