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Dog (Canine) Monoclonal AP2M1 Primary Antibody for ICC, IF - ABIN4280926
Jia, Xu, Qian, Yao, Miao, Zheng, Liu, Guo, Geng, Qiao, Liang: Identification of an endocytic signal essential for the antiviral action of IFITM3. in Cellular microbiology 2014
It has been shown that the cytoplasmic domains of furin bind the mu subunits of AP-1 and AP-2 in a phosphorylation-dependent manner.
AP2 has evolved as a key regulatory node to coordinate clarhtin-coated pit formation and cargo sorting and ensure high spatial and temporal regulation of cathrin-mediated endocytosis.
This study identified and confirmed adaptor protein 2 changes within the postsynaptic density in schizophrenia.
BMCC1 is an AP-2 associated endosomal protein in prostate cancer cells.
We identify dynamin and the EAP-binding alpha-adaptin appendage domain of the AP2 adaptor as switches in a regulated, multistep maturation process and provide direct evidence for a molecular checkpoint in clathrin mediated endocytosis.
a conserved heretofore unrecognized YXXPhi motif (Phi is a bulky hydrophobic residue) within the core protein. This motif is homologous to sorting signals within host cargo proteins known to mediate binding of AP2M1
Arkadia complexes with clathrin adaptor AP2 mu2 subunit and regulates EGF signalling.
These results suggest that AP-2 is essential for endocytic clathrin coated-pit and coated-vesicle formation.
multiple interactions between PIPKI gamma-p90 and AP-2 lead to spatiotemporally controlled PI(4,5)P(2) synthesis during clathrin-mediated synaptic vesicle endocytosis.
These results thus identify a novel type of AP-2 interaction determinant, support the notion that AP-2 is the key clathrin adaptor for the downregulation of CD4 by Nef, and reveal a previously unrecognized diversity among dileucine sorting signals.
These findings demonstrate differences in internalization between the alpha1a- and alpha1b-AR and provide evidence that the lack of significant endocytosis of the alpha1a-AR is linked to its poor interaction with beta-arrestins as well as with AP50.
The dyslexia-associated protein KIAA0319 interacts with adaptor protein 2 and follows the classical clathrin-mediated endocytosis pathway.
V1H can function as an adaptor for interactions between Nef and AP-2.
direct association of the adaptor complex 2 with a G protein-coupled receptor has not been reported so far and might represent a common mechanism underlying clathrin-mediated receptor endocytosis
Results indicate that AP-2 is not essential for clathrin-coated vesicle formation at the plasma membrane, but that it is one of several endocytic adaptors required for the uptake of certain cargo proteins.
AP-2 is completely dependent on both (D/E)xxxL(L/I) motifs and 20 YxxO motifs signals to mediate TCR internalization; AP2M1 interacts with tyrosine in CD3delta and CD3gamma
AP-2 and clathrin participate in MHC-II molecule trafficking to antigen-processing compartments.
We show that in addition to promoting LPA(1) signaling, membrane cholesterol is essential for the association of LPA(1) with beta-arrestin, which leads to signal attenuation and clathrin-dependent endocytosis of LPA(1).
Phosphorylation of AP-2 mu2 subunit is essential for Na+,K+-ATPase endocytosis in response to a variety of signals, such as dopamine or reactive oxygen species.
The essential GYxxtheta motif in the HIV-2 Env tail recruits AP-2 in order to direct Env to a cellular pathway or location that is necessary for its ability to enhance virus release.
Binding of AP-2 to otoferlin facilitates replenishment of release sites, for example, via speeding AZ clearance of exocytosed material, in addition to a role of AP-2 in synaptic vesicle reformation.
Data shsow that mutation of residues at the DEP-mu2 contact or in the tyrosine motif reduce affinity of Dvl2 for mu2.
This gene encodes a subunit of the heterotetrameric coat assembly protein complex 2 (AP2), which belongs to the adaptor complexes medium subunits family. The encoded protein is required for the activity of a vacuolar ATPase, which is responsible for proton pumping occurring in the acidification of endosomes and lysosomes. The encoded protein may also play an important role in regulating the intracellular trafficking and function of CTLA-4 protein. Two transcript variants encoding different isoforms have been found for this gene.
AP-2 complex subunit mu
, AP-2 mu 2 chain
, AP-2 mu chain
, HA2 50 kDA subunit
, adapter-related protein complex 2 mu subunit
, adaptor protein complex AP-2 subunit mu
, clathrin adaptor complex AP2, mu subunit
, clathrin assembly protein complex 2 medium chain
, clathrin coat adaptor protein AP50
, clathrin coat assembly protein AP50
, clathrin coat-associated protein AP50
, clathrin-associated/assembly/adaptor protein, medium 1
, plasma membrane adaptor AP-2 50 kDa protein
, plasma membrane adaptor AP-2 50kDA protein
, adaptor protein complex AP-2, mu1
, adaptor-related protein complex AP-2, mu1
, clathrin-associated AP-2
, coat assembly protein complex 50 kD
, AP-2 complex subunit mu-1-A
, AP-2 complex subunit mu-A
, AP-2 mu-2 chain A
, AP-2 mu-A chain
, clathrin assembly protein complex 2 medium chain A
, clathrin coat assembly protein AP50-A
, clathrin coat-associated protein AP50-A
, plasma membrane adaptor AP-2 50 kDa protein A
, AP-2 complex subunit mu-1-B
, AP-2 complex subunit mu-B
, AP-2 mu-2 chain B
, AP-2 mu-B chain
, clathrin assembly protein complex 2 medium chain B
, clathrin coat assembly protein AP50-B
, clathrin coat-associated protein AP50-B
, plasma membrane adaptor AP-2 50 kDa protein B
, AP-2 complex subunit mu-1
, AP-2 mu-2 chain
, HA2 50 kDa subunit
, adaptor-related protein complex 2, mu 1 subunit
, AP-2 complex subunit mu-like
, clathrin coat assembly protein ap50