Binding of AP2 to Sorting Signals Is Modulated by AP2 Phosphorylation
نویسندگان
چکیده
منابع مشابه
Phosphorylation of the AP2 μ subunit by AAK1 mediates high affinity binding to membrane protein sorting signals
During receptor-mediated endocytosis, AP2 complexes act as a bridge between the cargo membrane proteins and the clathrin coat by binding to sorting signals via the mu 2 subunit and to clathrin via the beta subunit. Here we show that binding of AP2 to sorting signals in vitro is regulated by phosphorylation of the mu 2 subunit of AP2. Phosphorylation of mu 2 enhances the binding affinity of AP2 ...
متن کاملSpecific DNA-binding by apicomplexan AP2 transcription factors.
Malaria remains one of the most prevalent infectious diseases worldwide, affecting more than half a billion people annually. Despite many years of research, the mechanisms underlying transcriptional regulation in the malaria-causing Plasmodium spp., and in Apicomplexan parasites generally, remain poorly understood. In Plasmodium, few regulatory elements sufficient to drive gene expression have ...
متن کاملAP-1 binding to sorting signals and release from clathrin-coated vesicles is regulated by phosphorylation
The adaptor protein complex-1 (AP-1) sorts and packages membrane proteins into clathrin-coated vesicles (CCVs) at the TGN and endosomes. Here we show that this process is highly regulated by phosphorylation of AP-1 subunits. Cell fractionation studies revealed that membrane-associated AP-1 differs from cytosolic AP-1 in the phosphorylation status of its beta1 and mu1 subunits. AP-1 recruitment ...
متن کاملAdipocyte Metabolism in Adipocyte Fatty Acid Binding Protein Knockout (aP2
Mice null for adipocyte fatty acid binding protein ( A FABP) compensate by increasing expression of keratinocyte fatty acid binding protein (KFABP) (Hotamisligil et al. S c i e n c e 274:1377–1379, 1996). In the present s t u d y, AFABP knockout (KO) and wild-type (WT) mice became equally obese on a high-fat diet, as judged by fat pad weights, adipocyte size, and body composition analysis. High...
متن کاملSulphur mustards inhibit binding of transcription factor AP2 in vitro.
The bifunctional sulphur mustard (bis-(2-chloroethyl)sulphide, HD) and its monofunctional analogue (2-chloroethyl ethyl sulphide, CEES) are both vesicants. In this study, both mustards were shown to rapidly alkylate the AP2 consensus binding sequence incorporated in a 26mer oligonucleotide. The reaction was essentially complete within 10 min under the conditions employed in this study and -95% ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2001
ISSN: 0021-9258
DOI: 10.1074/jbc.m009516200