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Titolo:
Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta - Regulation of nuclear localization by PDZ interactions
Autore:
Hogan, A; Shepherd, L; Chabot, J; Quenneville, S; Prescott, SM; Topham, MK; Gee, SH;
Indirizzi:
Univ Ottawa, Dept Cellular & Mol Med, Ctr Neuromusc Dis, Ottawa, ON K1H 8M5, Canada Univ Ottawa Ottawa ON Canada K1H 8M5 musc Dis, Ottawa, ON K1H 8M5, Canada Univ Utah, Huntsman Canc Inst, Salt Lake City, UT 84112 USA Univ Utah Salt Lake City UT USA 84112 Inst, Salt Lake City, UT 84112 USA Univ Utah, Dept Internal Med, Salt Lake City, UT 84112 USA Univ Utah SaltLake City UT USA 84112 l Med, Salt Lake City, UT 84112 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 28, volume: 276, anno: 2001,
pagine: 26526 - 26533
SICI:
0021-9258(20010713)276:28<26526:IOG1WD>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
DYSTROPHIN-ASSOCIATED PROTEIN; CENTRAL-NERVOUS-SYSTEM; NEUROMUSCULAR-JUNCTION; SODIUM-CHANNELS; SYNTROPHIN; DOMAIN; FAMILY; CLONING; MUSCLE; ALPHA-1-SYNTROPHIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: Gee, SH Univ Ottawa, Dept Cellular & Mol Med, Ctr Neuromusc Dis, 451 SmythRd, Ottawa, ON K1H 8M5, Canada Univ Ottawa 451 Smyth Rd Ottawa ON Canada K1H 8M5 K1H 8M5, Canada
Citazione:
A. Hogan et al., "Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta - Regulation of nuclear localization by PDZ interactions", J BIOL CHEM, 276(28), 2001, pp. 26526-26533

Abstract

Syntrophins are modular adapter proteins that link ion channels and signaling proteins to dystrophin and its homologues, A yeast two-hybrid screen ofa human brain cDNA library using the PDZ domain of gamma1-syntrophin, a recently identified brain-specific isoform, yielded overlapping clones encoding the C terminus of diacylglycerol kinase-zeta (DGK-zeta), an enzyme that converts diacylglycerol into phosphatidic acid, In biochemical assays, the C terminus of DGK-zeta, which contains a consensus PDZ-binding motif, was found to be necessary and sufficient for association with gamma1-syntrophin,When coexpressed in HeLa cells. DGK-zeta and gamma1-syntrophin formed a stable complex that partitioned between the cytoplasm and nucleus. DGK-zeta translocates from the cytosol to the nucleus, a process negatively regulatedby protein kinase C phosphorylation, We found that DGK-zeta recruits gamma1-syntrophin into the nucleus and that the PDZ-binding motif is required. Disrupting the interaction altered the intracellular localization of both proteins; DGK-zeta accumulated in the nucleus, whereas gamma1-syntrophin remained in the cytoplasm, The level of endogenous syntrophins in the nucleus of HeLa cells also reflected the amount of nuclear DGK-zeta, In the brain, DGK-zeta and gamma1-syntrophin were colocalized in cell bodies and dendritesof cerebellar Purkinjie neurons and other neuronal cell types, suggesting that their interaction is physiologically relevant. Moreover, coimmunoprecipitation and pull-down experiments from brain extracts and cells suggest that DGK-zeta, gamma1-syntrophin, and dystrophin form a ternary complex. Collectively, our results suggest that gamma1-syntrophin participates in regulating the subcellular localization of DGK-zeta to ensure correct terminationof diacylglycerol signaling.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 22:06:20