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Cited by 461

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A Comparative Analysis of the Phosphoinositide Binding Specificity of Pleckstrin Homology Domains

Open access
Rameh, Lucia E., Arvidsson, Ann-kristin, Carraway, Kermit L., Couvillon, Anthony D., Rathbun, Gary, Crompton, Anne, VanRenterghem, Barbara, Czech, Michael P., Ravichandran, Kodimangalam S., Burakoff, Steven J., Wang, Da-Sheng, Chen, Ching-Shih, Cantley, Lewis C.·1997·Journal of Biological Chemistry
DOI 10.1074/jbc.272.35.22059
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Abstract

Pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains are structurally related regulatory modules that are present in a variety of proteins involved in signal transduction, such as kinases, phospholipases, GTP exchange proteins, and adapter proteins. Initially these domains were shown to mediate protein-protein interactions, but more recently they were also found to bind phosphoinositides. Most studies to date have focused on binding of PH domains to phosphatidylinositol (PtdIns)-4-P and PtdIns-4,5-P2 and have not considered the lipid products of phosphoinositide 3-kinase: PtdIns-3-P, PtdIns-3,4-P2, and PtdIns-3,4,5-P3. Here we have compared the phosphoinositide specificity of six different PH domains and the Shc PTB domain using all five phosphoinositides. We show that the Bruton's tyrosine kinase PH domain binds to PtdIns-3,4, 5-P3 with higher affinity than to PtdIns-4,5-P2, PtdIns-3,4-P2 or inositol 1,3,4,5-tetrakisphosphate (Ins-1,3,4,5-P4). This selectivity is decreased by the xid mutation (R28C). Selective binding of PtdIns-3,4,5-P3 over PtdIns-4,5-P2 or PtdIns-3,4-P2 was also observed for the amino-terminal PH domain of T lymphoma invasion and metastasis protein (Tiam-1), the PH domains of Son-of-sevenless (Sos) and, to a lesser extent, the PH domain of the beta-adrenergic receptor kinase. The oxysterol binding protein and beta-spectrin PH domains bound PtdIns-3,4,5-P3 and PtdIns-4,5-P2 with similar affinities. PtdIns-3,4,5-P3 and PtdIns-4,5-P2 also bound to the PTB domain of Shc with similar affinities and lipid binding was competed with phosphotyrosine (Tyr(P)-containing peptides. These results indicate that distinct PH domains select for different phosphoinositides.

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Authors
Rameh, L. E., Arvidsson, A.-K., Carraway, K. L., Couvillon, A. D., Rathbun, G., Crompton, A., VanRenterghem, B., Czech, M. P., Ravichandran, K. S., Burakoff, S. J., Wang, D.-S., Chen, C.-S., & Cantley, L. C.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1997-08
Volume
272
Issue
35
Pages
22059-22066
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.272.35.22059
OpenAlex
W2132382863
Cited by
461
References
2
FWCI
20.59
Type
journal article
Language
en
Open access
hybrid

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