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Titolo:
Inhibition of phospholipase D by amphiphysins
Autore:
Lee, C; Kim, SR; Chung, JK; Frohman, MA; Kilimann, MW; Rhee, SG;
Indirizzi:
NHLBI, Lab Cell Signaling, NIH, Bethesda, MD 20892 USA NHLBI Bethesda MD USA 20892 b Cell Signaling, NIH, Bethesda, MD 20892 USA SUNY Stony Brook, Dept Pharmacol Sci, Stony Brook, NY 11794 USA SUNY StonyBrook Stony Brook NY USA 11794 Sci, Stony Brook, NY 11794 USA Ruhr Univ Bochum, Inst Physiol Chem, D-44780 Bochum, Germany Ruhr Univ Bochum Bochum Germany D-44780 ol Chem, D-44780 Bochum, Germany
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 25, volume: 275, anno: 2000,
pagine: 18751 - 18758
SICI:
0021-9258(20000623)275:25<18751:IOPDBA>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADP-RIBOSYLATION-FACTOR; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN; CLATHRIN-MEDIATED ENDOCYTOSIS; SECRETORY VESICLE FORMATION; PHOSPHATIDIC-ACID; INOSITIDE PHOSPHORYLATION; LYSOPHOSPHATIDIC ACID; NERVE-TERMINALS; PLASMA-MEMBRANE; BINDING-SITE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Rhee, SG NHLBI, Lab Cell Signaling, NIH, Bldg 3,Rm 120,3 Ctr Dr,MSC 0320, Bethesda,MD 20892 USA NHLBI Bldg 3,Rm 120,3 Ctr Dr,MSC 0320 Bethesda MD USA20892 2 USA
Citazione:
C. Lee et al., "Inhibition of phospholipase D by amphiphysins", J BIOL CHEM, 275(25), 2000, pp. 18751-18758

Abstract

Two distinct proteins inhibiting phospholipase D (PLD) activity in rat brain cytosol were previously purified and identified as synaptojanin and AP180, which are specific to nerve terminals and associate with the clathrin coat. Two additional PLD-inhibitory proteins have now been purified and identified as the amphiphysins I and II, which forms a heterodimer that also associates with the clathrin coat. Bacterially expressed recombinant amphiphysins inhibited both PLD1 and PLDS isozymes in vitro with a potency similar to that of brain amphiphysin (median inhibitory concentration of similar to 15 nM). Expressions of either amphiphysin in COS-7 cells reduced activity of endogenous PLD as well as exogenously expressed PLD1 and PLD2, Coprecipitation experiments suggested that the inhibitory effect of amphiphysins results from their direct interaction with PLDs. The NH2 terminus of amphiphysin I was critical for both inhibition of and binding to PLD. Phosphatidic acid formed by signal-induced PLD is thought to be required for the assembly of clathrin-coated vesicles during endocytosis, Thus, the inhibition of PLDby amphiphysins, synaptojanin, and AP180 might play an important role in synaptic vesicle trafficking.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/04/20 alle ore 15:57:59