Sorting nexin: Difference between revisions
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<StructureSection load='3dyt' size='350' side='right' caption='Structure of human sorting nexin-9 PX domain complex with sulfate (PDB entry [[3dyt]])' scene=''> | <StructureSection load='3dyt' size='350' side='right' caption='Structure of human sorting nexin-9 PX domain complex with sulfate (PDB entry [[3dyt]])' scene=''> | ||
== Function == | |||
'''Sorting nexins''' (SNX) are proteins which enhance membrane association via their lipid-binding PX domain or via protein-protein association. The PX domain contains a phospholipid-binding motif. | '''Sorting nexins''' (SNX) are proteins which enhance membrane association via their lipid-binding PX domain or via protein-protein association<ref>PMID:25619244</ref>. The PX domain contains a phospholipid-binding motif. | ||
*'''SNX 1''' regulates trafficking in the endosome compartment<ref>PMID:11997453</ref>.<br /> | |||
*'''SNX 3''' regulates neurite formation<ref>PMID:19576982</ref>.<br /> | |||
*'''SNX 5''' regulates retrograde trafficking of transmembrane cargo receptors<ref>PMID:19553671</ref>.<br /> | |||
== Relevance == | |||
SNX 2 is a potential marker of hyper functioning thyroid disorders<ref>PMID:23531855</ref>. | |||
</StructureSection> | </StructureSection> | ||
| Line 78: | Line 85: | ||
**[[3hpb]], [[3hpc]] – rSNX PX domain – rat<br /> | **[[3hpb]], [[3hpc]] – rSNX PX domain – rat<br /> | ||
}} | }} | ||
== References == | |||
<references/> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 13:26, 30 August 2016
FunctionSorting nexins (SNX) are proteins which enhance membrane association via their lipid-binding PX domain or via protein-protein association[1]. The PX domain contains a phospholipid-binding motif.
RelevanceSNX 2 is a potential marker of hyper functioning thyroid disorders[5]. |
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3D structures of sorting nexin3D structures of sorting nexin
Updated on 30-August-2016
ReferencesReferences
- ↑ Gallon M, Cullen PJ. Retromer and sorting nexins in endosomal sorting. Biochem Soc Trans. 2015 Feb;43(1):33-47. doi: 10.1042/BST20140290. PMID:25619244 doi:http://dx.doi.org/10.1042/BST20140290
- ↑ Zhong Q, Lazar CS, Tronchere H, Sato T, Meerloo T, Yeo M, Songyang Z, Emr SD, Gill GN. Endosomal localization and function of sorting nexin 1. Proc Natl Acad Sci U S A. 2002 May 14;99(10):6767-72. Epub 2002 May 7. PMID:11997453 doi:http://dx.doi.org/10.1073/pnas.092142699
- ↑ Mizutani R, Yamauchi J, Kusakawa S, Nakamura K, Sanbe A, Torii T, Miyamoto Y, Tanoue A. Sorting nexin 3, a protein upregulated by lithium, contains a novel phosphatidylinositol-binding sequence and mediates neurite outgrowth in N1E-115 cells. Cell Signal. 2009 Nov;21(11):1586-94. doi: 10.1016/j.cellsig.2009.06.005. Epub, 2009 Jul 2. PMID:19576982 doi:http://dx.doi.org/10.1016/j.cellsig.2009.06.005
- ↑ Koharudin LM, Furey W, Liu H, Liu YJ, Gronenborn AM. The phox domain of sorting nexin 5 lacks phosphatidylinositol 3-phosphate (PtdIns(3)P) specificity and preferentially binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). J Biol Chem. 2009 Aug 28;284(35):23697-707. Epub 2009 Jun 24. PMID:19553671 doi:http://dx.doi.org/M109.008995
- ↑ Kanzawa M, Hara S, Semba S, Yokozaki H, Hirokawa M, Itoh T. Sorting Nexin 2 (SNX2): a potential marker of active thyrocytes in normal and hyperfunctioning thyroid disorders. Appl Immunohistochem Mol Morphol. 2014 Apr;22(4):302-7. doi:, 10.1097/PAI.0b013e31828badd3. PMID:23531855 doi:http://dx.doi.org/10.1097/PAI.0b013e31828badd3