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Volumn 11, Issue 11, 2001, Pages 896-900

Phosphorylation of threonine 156 of the μ2 subunit of the AP2 complex is essential for endocytosis in vitro and in vivo

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EID: 0035810915     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(01)00240-8     Document Type: Article
Times cited : (121)

References (31)
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    • Clathrin-coated vesicles contain 2 protein-kinase activities - Phosphorylation of clathrin β-light chain by casein kinase-II
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  • 9
  • 13
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    • The 50 kDa protein subunit of assembly polypeptide (AP) AP-2 adaptor from clathrin-coated vesicles is phosphorylated on threonine-156 by AP-1 and a soluble ap50 kinase which copurifies with the assembly polypeptides
    • (1993) Biochem J , vol.296 , pp. 409-415
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    • A structural explanation for the recognition of tyrosine-based endocytotic signals
    • (1998) Science , vol.282 , pp. 1327-1332
    • Owen, D.J.1    Evans, P.R.2
  • 21
    • 0033002138 scopus 로고    scopus 로고
    • Phosphorylation of the medium chain subunit of the AP-2 adaptor complex does not influence its interaction with the tyrosine based internalisation motif of TGN38
    • (1999) FEBS Lett , vol.444 , pp. 195-200
    • Crump, C.M.1    Banting, G.2
  • 28
    • 0023645502 scopus 로고
    • Purification and characterization of 2 distinct complexes of assembly polypeptides from calf brain coated vesicles that differ in their polypeptide composition and kinase-activities
    • (1987) J Biol Chem , vol.262 , pp. 12182-12188
    • Manfredi, J.J.1    Bazari, W.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.