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Adaptor protein complex AP-2, mu1

clathrin-associated AP-2
Top mentioned proteins: p15, CAN, ACID, V1a, CD45
Papers on clathrin-associated AP-2
Structural analysis of the interaction between Dishevelled2 and clathrin AP-2 adaptor, a critical step in noncanonical Wnt signaling.
Kirchhausen et al., Boston, United States. In Structure, 2010
Data shsow that mutation of residues at the DEP-mu2 contact or in the tyrosine motif reduce affinity of Dvl2 for mu2.
Internalization of pseudorabies virus glycoprotein B is mediated by an interaction between the YQRL motif in its cytoplasmic domain and the clathrin-associated AP-2 adaptor complex.
Nauwynck et al., Merelbeke, Belgium. In J Virol, 2004
Furthermore, we found that PRV gB colocalizes with the cellular clathrin-associated AP-2 adaptor complex and that this colocalization depends on the YQRL motif.
The role of endocytic l1 trafficking in polarized adhesion and migration of nerve growth cones.
Yoshihara et al., Wako, Japan. In J Neurosci, 2002
This gradient of L1 adhesion is attenuated after inhibition of L1 endocytosis in the growth cone by intracellular loading of a function-blocking antibody against alpha-adaptin, a subunit of the clathrin-associated AP-2 adaptor.
An internalization-competent influenza hemagglutinin mutant causes the redistribution of AP-2 to existing coated pits and is colocalized with AP-2 in clathrin free clusters.
Petersen et al., London, Canada. In Biochemistry, 1999
While such complexes can in principle serve to recruit clathrin for the formation of new coated pits, the higher affinity of the internalization signals for clathrin-associated AP-2 [Rapoport, I., et al. (1997) EMBO J. 16, 2240-2250] makes it more likely that once the AP-2-membrane protein complexes form, they are quickly recruited into existing coated pits.
Phosphoinositide-AP-2 interactions required for targeting to plasma membrane clathrin-coated pits.
Keen et al., Philadelphia, United States. In J Cell Biol, 1999
The clathrin-associated AP-2 adaptor protein is a major polyphosphoinositide-binding protein in mammalian cells.
The role of lipid signaling in constitutive membrane traffic.
Sternweis et al., Dallas, United States. In Curr Opin Cell Biol, 1997
Recent evidence suggests that specific phosphatidylinositides may regulate the activity of proteins with diverse functions in membrane transport, such as dynamin, the clathrin-associated AP-2 complex, and proteins that stimulate guanine nucleotide exchange on ADP-ribosylation factors (ARFs).
An interaction between inositol hexakisphosphate (IP6) and insulin-like growth factor II receptor binding sites in the rat brain.
Parent et al., Montréal, Canada. In Neuroreport, 1994
These results, in keeping with other evidence, suggest that IP6 may be able to regulate the [125I]IGF II receptor binding sites either directly or indirectly, possibly through clathrin-associated AP-2 sites.
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