| Structural highlights
Function
PDLI7_HUMAN May function as a scaffold on which the coordinated assembly of proteins can occur. May play a role as an adapter that, via its PDZ domain, localizes LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. Involved in both of the two fundamental mechanisms of bone formation, direct bone formation (e.g. embryonic flat bones mandible and cranium), and endochondral bone formation (e.g. embryonic long bone development). Plays a role during fracture repair. Involved in BMP6 signaling pathway (By similarity).[1] [2] SNX17_HUMAN Critical regulator of endosomal recycling of numerous receptors, channels, and other transmembrane proteins. Binds to NPxY sequences in the cytoplasmic tails of target cargos. Plays a role in the sorting of endocytosed LRP1 and APP, and prevents their degradation. Required for maintenance of normal cell surface levels of APP and LRP1. Recycles internalized integrins ITGB1, ITGB5 and their associated alpha subunits, preventing them from lysosomal degradation. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)).[3] [4] [5] [6] [7] [8]
References
- ↑ Wu RY, Gill GN. LIM domain recognition of a tyrosine-containing tight turn. J Biol Chem. 1994 Oct 7;269(40):25085-90. PMID:7929196
- ↑ Liu Y, Hair GA, Boden SD, Viggeswarapu M, Titus L. Overexpressed LIM mineralization proteins do not require LIM domains to induce bone. J Bone Miner Res. 2002 Mar;17(3):406-14. PMID:11874232
- ↑ Williams R, Schluter T, Roberts MS, Knauth P, Bohnensack R, Cutler DF. Sorting nexin 17 accelerates internalization yet retards degradation of P-selectin. Mol Biol Cell. 2004 Jul;15(7):3095-105. Epub 2004 Apr 30. PMID:15121882 doi:10.1091/mbc.E04-02-0143
- ↑ Knauth P, Schluter T, Czubayko M, Kirsch C, Florian V, Schreckenberger S, Hahn H, Bohnensack R. Functions of sorting nexin 17 domains and recognition motif for P-selectin trafficking. J Mol Biol. 2005 Apr 8;347(4):813-25. PMID:15769472 doi:S0022-2836(05)00144-0
- ↑ Czubayko M, Knauth P, Schluter T, Florian V, Bohnensack R. Sorting nexin 17, a non-self-assembling and a PtdIns(3)P high class affinity protein, interacts with the cerebral cavernous malformation related protein KRIT1. Biochem Biophys Res Commun. 2006 Jul 7;345(3):1264-72. Epub 2006 May 2. PMID:16712798 doi:10.1016/j.bbrc.2006.04.129
- ↑ Donoso M, Cancino J, Lee J, van Kerkhof P, Retamal C, Bu G, Gonzalez A, Caceres A, Marzolo MP. Polarized traffic of LRP1 involves AP1B and SNX17 operating on Y-dependent sorting motifs in different pathways. Mol Biol Cell. 2009 Jan;20(1):481-97. doi: 10.1091/mbc.E08-08-0805. Epub 2008 Nov, 12. PMID:19005208 doi:10.1091/mbc.E08-08-0805
- ↑ Steinberg F, Heesom KJ, Bass MD, Cullen PJ. SNX17 protects integrins from degradation by sorting between lysosomal and recycling pathways. J Cell Biol. 2012 Apr 16;197(2):219-30. doi: 10.1083/jcb.201111121. Epub 2012 Apr, 9. PMID:22492727 doi:10.1083/jcb.201111121
- ↑ Ghai R, Mobli M, Norwood SJ, Bugarcic A, Teasdale RD, King GF, Collins BM. Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Proc Natl Acad Sci U S A. 2011 Apr 21. PMID:21512128 doi:10.1073/pnas.1017110108
|
