A site of interaction between pleckstrin's PH domains and G beta gamma.
Biochim Biophys Acta
; 1314(3): 233-8, 1996 Dec 12.
Article
em En
| MEDLINE
| ID: mdl-8982277
ABSTRACT
Pleckstrin is a 40 kDa substrate for protein kinase C found in platelets and neutrophils. Based upon its sequence, pleckstrin contains two of the recently-described PH domains that are thought to be binding motifs for phosphatidyl 4,5-bisphosphate (PIP2) and/or G protein beta gamma heterodimers (G beta gamma). In the present studies we have examined the interaction between pleckstrin and G beta gamma by incubating pleckstrin fusion proteins with lysates from human platelets. In this analysis, both the N-terminal and C-terminal PH domains from pleckstrin bound G beta gamma in vitro, as did peptides containing as little as the first 30 residues of the C-terminal pleckstrin PH domain. Introduction of a point mutation into this region, analogous to the mutation in the Btk PH domain that causes X-linked immunodeficiency disease (XID) in mice, dramatically disrupted this interaction. We propose that pleckstrin may interact with G beta gamma, and that one potential site for this interaction involves the first 30 residues of pleckstrin's C-terminal PH domain.
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Base de dados:
MEDLINE
Assunto principal:
Fosfoproteínas
/
Proteínas Sanguíneas
/
Homologia de Sequência de Aminoácidos
/
Proteínas de Ligação ao GTP
Limite:
Humans
Idioma:
En
Ano de publicação:
1996
Tipo de documento:
Article