Anti-SNX6 Antibody Picoband® Fluoro647 Conjugated

This gene encodes a member of the sorting nexin family. Members of this family contain a phox (PX) domain, which is a phosphoinositide binding domain, and are involved in intracellular trafficking. This protein associates with the long isoform of the leptin receptor, the transforming growth factor-beta family of receptor serine-threonine kinases, and with receptor tyrosine kinases for platelet-derived growth factor, insulin, and epidermal growth factor. This protein may form oligomeric complexes with family member proteins through interactions of both the PX domain and the coiled coil regions of the molecules. Translocation of this protein from the cytoplasm to the nucleus occurs after binding to proviral integration site 1 protein. This gene results in two transcripts encoding two distinct isoforms.

AP-2 complex subunit beta; AP105B; Adaptor protein complex AP-2 subunit beta; Adaptor-related protein complex 2 subunit beta; Beta-2-adaptin; Beta-adaptin; Clathrin assembly protein complex 2 beta large chain; Plasma membrane adaptor HA2/AP2 adaptin beta subunit; AP2B1; ADTB2, CLAPB1

Component of the adaptor protein complex 2 (AP-2) . Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin- coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind ly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind ly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins; at least some clathrin- associated sorting proteins (CLASPs) are recognized by their [DE]- X (1,2) -F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly; clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly. .

1. Chen, D., Xiao, H., Zhang, K., Wang, B., Gao, Z., Jian, Y., Qi, X., Sun, J., Miao, L., Yang, C. Retromer is required for apoptotic cell clearance by phagocytic receptor recycling. Science 327: 1261-1264, 2010. 2. Parks, W. T., Frank, D. B., Huff, C., Haft, C. R., Martin, J., Meng, X., de Caestecker, M. P., McNally, J. G., Reddi, A., Taylor, S. I., Roberts, A. B., Wang, T., Lechleider, R. J. Sorting nexin 6, a novel SNX, interacts with the transforming growth factor-beta family of receptor serine-threonine kinases. J. Biol. Chem. 276: 19332-19339, 2001.

Cell membrane . Membrane, coated pit ; Peripheral membrane protein ; Cytoplasmic side . AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV.