Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Binding of AP2 to sorting signals is modulated by AP2 phosphorylation
Autore:
Fingerhut, A; von Figura, K; Honing, S;
Indirizzi:
Univ Gottingen, Inst Biochem 2, D-37073 Gottingen, Germany Univ GottingenGottingen Germany D-37073 m 2, D-37073 Gottingen, Germany
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 8, volume: 276, anno: 2001,
pagine: 5476 - 5482
SICI:
0021-9258(20010223)276:8<5476:BOATSS>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
CLATHRIN-COATED VESICLES; LYSOSOMAL ACID-PHOSPHATASE; MEDIATED ENDOCYTOSIS; UNCOATING ATPASE; ARRESTIN/CLATHRIN INTERACTION; ASSEMBLY POLYPEPTIDES; CYTOPLASMIC DOMAIN; KINASE-ACTIVITIES; INVITRO BINDING; TERMINAL DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Honing, S Univ Gottingen, Inst Biochem 2, Heinrich Duker Weg 12, D-37073 Gottingen, Germany Univ Gottingen Heinrich Duker Weg 12 Gottingen Germany D-37073
Citazione:
A. Fingerhut et al., "Binding of AP2 to sorting signals is modulated by AP2 phosphorylation", J BIOL CHEM, 276(8), 2001, pp. 5476-5482

Abstract

The two clathrin-associated adaptor complexes API and AP2 are known to participate in the formation of clathrin-coated vesicles at the trans-Golgi network and at the plasma membrane. During this process adaptors are involvedin the sequestration of vesicle cargo by binding to the sorting signals within the cytoplasmic domains of the cargo proteins and in the recruitment of the clathrin coat. After budding of the clathrin-coated vesicles, the clathrin and adaptors dissociate from the vesicles. Here we show that in vitrobinding of AP2 to sorting signals, which is one of the initial steps in receptor-mediated endocytosis, is modulated by adaptor phosphorylation. AP2 was phosphorylated by incubating purified AP2 in the presence of ATP and dephosphorylated by incubation with alkaline phosphatase. Affinity for tyrosine-, leucine-based and noncanonical sorting motifs was 15-33 times higher for phosphorylated than for dephosphorylated AP2. Also the binding of AP2 to membranes was regulated by adaptor phosphorylation/dephosphorylation and was about 8-fold higher for phosphorylated than for dephosphorylated AP2. Moreover, AP2 isolated from cytosol is higher phosphorylated than membrane-extracted and exhibits a B-fold higher binding affinity than AP2 extracted from membranes. Taken together these data point to a cycle of phosphorylation/dephosphorylation as a mechanism for regulating the reversible association of AP2 with membranes and sorting signals during the process of recptor-mediated endocytosis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/20 alle ore 03:58:14