메뉴 건너뛰기




Volumn 156, Issue 5, 2002, Pages 791-795

Phosphorylation of the AP2 μ subunit by AAK1 mediates high affinity binding to membrane protein sorting signals

Author keywords

Clathrin; Coated vesicle; Endocytosis; Receptor; Trafficking

Indexed keywords

ADAPTOR PROTEIN; CLATHRIN; MEMBRANE PROTEIN; PHOSPHOTRANSFERASE; PROTEIN AAK1; PROTEIN SUBUNIT; THREONINE; TRANSCRIPTION FACTOR AP 2; UNCLASSIFIED DRUG;

EID: 0037018156     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200111068     Document Type: Article
Times cited : (222)

References (18)
  • 2
    • 0023001146 scopus 로고
    • Clathrin-coated vesicles contain two protein kinase activities. Phosphorylation of clathrin beta-light chain by casein kinase II
    • (1986) J. Biol. Chem. , vol.261 , pp. 9614-9621
    • Bar-Zvi, D.1    Branton, D.2
  • 12
    • 0032514874 scopus 로고    scopus 로고
    • A structural explanation for the recognition of tyrosine-based endocytotic signals
    • (1998) Science , vol.282 , pp. 1327-1332
    • Owen, D.1    Evans, P.2
  • 13
    • 0027370730 scopus 로고
    • The 50 kDa protein subunit of assembly polypepride (AP) AP-2 adaptor from clathrin-coated vesicles is phosphorylated on rhreonine-156 by AP-1 and a soluble AP50 kinase which co-purifies with the assembly polypeptides
    • (1993) Biochem. J. , vol.296 , pp. 409-415
    • Pauloin, A.1    Thurieau, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.