Pleckstrin homology domains: A common fold with diverse functions

被引：247

作者：

Rebecchi, MJ ^{[1
]}

Scarlata, S

机构：

[1] SUNY Stony Brook, Dept Anesthesiol, Stony Brook, NY 11794 USA

[2] SUNY Stony Brook, Dept Physiol & Biophys, Stony Brook, NY 11794 USA

来源：

ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE | 1998年 / 27卷

关键词：

protein motifs; protein modules; membrane binding; phosphoinositides; G proteins;

D O I：

10.1146/annurev.biophys.27.1.503

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Pleckstrin homology (PH) motifs are approximately 100 amino-acid residues long and have been identified in nearly 100 different eukaryotic proteins, many of which participate in cell signaling and cytoskeletal regulation. Despite minimal sequence homology, the three-dimensional structures are remarkably conserved. This review gives an overview of the PH domain architecture and examines the best-studied examples in an attempt to understand their function.

引用

页码：503 / +

页数：27

共 107 条

[1] PROTEIN-KINASE-C REGULATES PLECKSTRIN BY PHOSPHORYLATION OF SITES ADJACENT TO THE N-TERMINAL PLECKSTRIN HOMOLOGY DOMAIN [J].

ABRAMS, CS ;

ZHAO, W ;

BELMONTE, E ;

BRASS, LF .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (40) :23317-23321

[2] Phosphopleckstrin inhibits G beta gamma-activable platelet phosphatidylinositol-4,5-bisphosphate 3-kinase [J].

Abrams, CS ;

Zhang, J ;

Downes, CP ;

Tang, XW ;

Zhao, W ;

Rittenhouse, SE .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (41) :25192-25197

[3] A site of interaction between pleckstrin's PH domains and G(beta gamma) [J].

Abrams, CS ;

Zhao, W ;

Brass, LF .

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 1996, 1314 (03) :233-238

[4] PLECKSTRIN INHIBITS PHOSPHOINOSITIDE HYDROLYSIS INITIATED BY G-PROTEIN-COUPLED AND GROWTH-FACTOR RECEPTORS - A ROLE FOR PLECKSTRINS PH DOMAINS [J].

ABRAMS, CS ;

WU, H ;

ZHAO, W ;

BELMONTE, E ;

WHITE, D ;

BRASS, LF .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (24) :14485-14492

[5] Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase B alpha [J].

Alessi, DR ;

James, SR ;

Downes, CP ;

Holmes, AB ;

Gaffney, PRJ ;

Reese, CB ;

Cohen, P .

CURRENT BIOLOGY, 1997, 7 (04) :261-269

[6] MEMBRANE TARGETING OF THE NUCLEOTIDE EXCHANGE FACTOR SOS IS SUFFICIENT FOR ACTIVATING THE RAS SIGNALING PATHWAY [J].

ARONHEIM, A ;

ENGELBERG, D ;

LI, NX ;

ALALAWI, N ;

SCHLESSINGER, J ;

KARIN, M .

CELL, 1994, 78 (06) :949-961

[7] Specific role for the PH domain of dynamin-1 in the regulation of rapid endocytosis in adrenal chromaffin cells [J].

Artalejo, CR ;

Lemmon, MA ;

Schlessinger, J ;

Palfrey, HC .

EMBO JOURNAL, 1997, 16 (07) :1565-1574

[8] A single amino acid substitution in the pleckstrin homology domain of phospholipase C delta 1 enhances the rate of substrate hydrolysis [J].

Bromann, PA ;

Boetticher, EE ;

Lomasney, JW .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (26) :16240-16246

[9] COMPARISON OF THE LEVELS OF INOSITOL METABOLITES IN TRANSFORMED HEMATOPOIETIC-CELLS AND THEIR NORMAL COUNTERPARTS [J].

BUNCE, CM ;

FRENCH, PJ ;

ALLEN, P ;

MOUNTFORD, JC ;

MOOR, B ;

GREAVES, MF ;

MICHELL, RH ;

BROWN, G .

BIOCHEMICAL JOURNAL, 1993, 289 :667-673

[10] Focal adhesions, contractility, and signaling [J].

Burridge, K ;

ChrzanowskaWodnicka, M .

ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, 1996, 12 :463-518

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