Pleckstrin

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Pleckstrin-1
Chr. 2 p13.3
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StructuresSwiss-model
DomainsInterPro
Chr. 14 q23.3q24.1
WikidataQ18038260
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StructuresSwiss-model
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Pleckstrins are a family of

leukocyte C kinase substrate and the KSTR string of amino acids. The prototype protein, now called pleckstrin-1, was first identified in 1979 as the major substrate of protein kinase C in platelets.[2] The homolog pleckstrin-2 is more widely expressed in tissues.[3]

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

F-actin, unlike pleckstrin-1.[3]
Since pleckstrin-2 is expressed in a wider variety of cell types, its biological roles are more diverse than those of pleckstrin-1.

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

epithelial-to-mesenchymal transition in tumor metastasis, and pleckstrin-2 is known to be overexpressed in a variety of cancers.[3]

References

External links