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Publication : A testis-specific regulator of complex and hybrid N-glycan synthesis.

First Author  Huang HH Year  2010
Journal  J Cell Biol Volume  190
Issue  5 Pages  893-910
PubMed ID  20805325 Mgi Jnum  J:240589
Mgi Id  MGI:5887193 Doi  10.1083/jcb.201004102
Citation  Huang HH, et al. (2010) A testis-specific regulator of complex and hybrid N-glycan synthesis. J Cell Biol 190(5):893-910
abstractText  Database analyses identified 4933434I20Rik as a glycosyltransferase-like gene expressed mainly in testicular germ cells and regulated during spermatogenesis. Expression of a membrane-bound form of the protein resulted in a marked and specific reduction in N-acetylglucosaminyltransferase I (GlcNAcT-I) activity and complex and hybrid N-glycan synthesis. Thus, the novel activity was termed GlcNAcT-I inhibitory protein (GnT1IP). Membrane-bound GnT1IP localizes to the ER, the ER-Golgi intermediate compartment (ERGIC), and the cis-Golgi. Coexpression of membrane-anchored GnT1IP with GlcNAcT-I causes association of the two proteins, inactivation of GlcNAcT-I, and mislocalization of GlcNAcT-I from the medial-Golgi to earlier compartments. Therefore, GnT1IP is a regulator of GlcNAcT-I and complex and hybrid N-glycan production. Importantly, the formation of high mannose N-glycans resulting from inhibition of GlcNAcT-I by GnT1IP markedly increases the adhesion of CHO cells to TM4 Sertoli cells. Testicular germ cells might use GnT1IP to induce the expression of high mannose N-glycans on glycoproteins, thereby facilitating Sertoli-germ cell attachment at a particular stage of spermatogenesis.
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