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 co-purifies with the assembly polypeptides.
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Summary
It was demonstrated that AP50 was a phosphorylation substrate unable to autophosphorylate, shown to be associated with AP-1 and with a soluble protein complex co-purified with APs but resolved from the latter by hydroxyapatite-column exclusion chromatography.
- Type
- article
- Published
- 1993-12-01
- Cited by
- 36
- References
- 0
- Access
- Open access
- OpenAlex
- https://openalex.org/W49587981
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:24943374
Keywords
Phosphorylation, Threonine, Biology, Protein subunit, Biochemistry
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Cited by
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- CK2 and GAK/auxilin2 Are Major Protein Kinases in Clathrin‐Coated Vesicles
- Clathrin promotes incorporation of cargo into coated pits by activation of the AP2 adaptor μ2 kinase
- Phosphatidylinositol-(4,5)-bisphosphate regulates sorting signal recognition by the clathrin-associated adaptor complex AP2.
- Suppressors of YCK‐encoded yeast casein kinase 1 deficiency define the four subunits of a novel clathrin AP‐like complex
- Binding of AP2 to Sorting Signals Is Modulated by AP2 Phosphorylation*
- Phosphorylation of threonine 156 of the μ2 subunit of the AP2 complex is essential for endocytosis in vitro and in vivo
- Casein Kinase II Activity Is Required for Transferrin Receptor Endocytosis*
- Phosphorylation of the AP2 μ subunit by AAK1 mediates high affinity binding to membrane protein sorting signals
- Interactions between HIV1 Nef and vacuolar ATPase facilitate the internalization of CD4.
- Regulating the clathrin-coated vesicle cycle by AP2 subunit phosphorylation.
- Life of a clathrin coat: insights from clathrin and AP structures
- The Ark1/Prk1 family of protein kinases. Regulators of endocytosis and the actin skeleton.
- Casein Kinase II Sites in the Intracellular C-terminal Domain of the Thyrotropin-releasing Hormone Receptor and Chimeric Gonadotropin-releasing Hormone Receptors Contribute to β-Arrestin-dependent Internalization*
- The membrane-associated proteins FCHo and SGIP are allosteric activators of the AP2 clathrin adaptor complex
- Organization of signaling networks during receptor-mediated membrane protein trafficking
- Coordinated regulation of AP2 uncoating from clathrin-coated vesicles by rab5 and hRME-6
- Molecular architecture and functional model of the endocytic AP2 complex.
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