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Titolo:
A conserved clathrin assembly motif essential for synaptic vesicle endocytosis
Autore:
Morgan, JR; Prasad, K; Hao, WH; Augustine, GJ; Lafer, EM;
Indirizzi:
Duke Univ, Med Ctr, Dept Neurobiol, Durham, NC 27710 USA Duke Univ DurhamNC USA 27710 d Ctr, Dept Neurobiol, Durham, NC 27710 USA Univ Texas, Hlth Sci Ctr, Dept Biochem, San Antonio, TX 78229 USA Univ Texas San Antonio TX USA 78229 pt Biochem, San Antonio, TX 78229 USA Marine Biol Lab, Woods Hole, MA 02543 USA Marine Biol Lab Woods Hole MA USA 02543 iol Lab, Woods Hole, MA 02543 USA
Titolo Testata:
JOURNAL OF NEUROSCIENCE
fascicolo: 23, volume: 20, anno: 2000,
pagine: 8667 - 8676
SICI:
0270-6474(200012)20:23<8667:ACCAME>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
AP-3 ADAPTER COMPLEX; COATED VESICLES; PROTEIN AP-3; ARRESTIN/CLATHRIN INTERACTION; MONOCLONAL-ANTIBODIES; PLASMA-MEMBRANE; TERMINAL DOMAIN; BINDING DOMAIN; ALPHA-ADAPTIN; F1-20 PROTEIN;
Keywords:
AP180; AP-2; clathrin adaptors; coated vesicles; membrane trafficking; presynaptic terminals; synaptic transmission;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Augustine, GJ Duke Univ, Med Ctr, Dept Neurobiol, Box 3209, Durham, NC 27710 USA Duke Univ Box 3209 Durham NC USA 27710 Durham, NC 27710 USA
Citazione:
J.R. Morgan et al., "A conserved clathrin assembly motif essential for synaptic vesicle endocytosis", J NEUROSC, 20(23), 2000, pp. 8667-8676

Abstract

Although clathrin assembly by adaptor proteins (APs) plays a major role inthe recycling of synaptic vesicles, the molecular mechanism that allows APs to assemble clathrin is poorly understood. Here we demonstrate that AP180, like AP-2 and AP-3, binds to the N-terminal domain of clathrin. Sequence analysis reveals a motif, containing the sequence DLL, that exists in multiple copies in many clathrin APs. Progressive deletion of these motifs caused a gradual reduction in the ability of AP180 to assemble clathrin in vitro. Peptides from AP180 or AP-2 containing this motif also competitively inhibited clathrin assembly by either protein. Microinjection of these peptidesinto squid giant presynaptic terminals reversibly blocked synaptic transmission and inhibited synaptic vesicle endocytosis by preventing coated pit formation at the plasma membrane. These results indicate that the DLL motif confers clathrin assembly properties to AP180 and AP-2 and, perhaps, to other APs. We propose that APs promote clathrin assembly by cross-linking clathrin triskelia via multivalent interactions between repeated DLL motifs in the APs and complementary binding sites on the N-terminal domain of clathrin. These results reveal the structural basis for clathrin assembly and provide novel insights into the molecular mechanism of clathrin-mediated synaptic vesicle endocytosis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/09/20 alle ore 14:00:56