BAIT

ALG14

N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase anchoring subunit ALG14, YBR070C
Component of UDP-GlcNAc transferase; required for the second step of dolichyl-linked oligosaccharide synthesis; anchors the catalytic subunit Alg13p to the ER membrane; similar to bacterial and human glycosyltransferases
Saccharomyces cerevisiae (S288c)
PREY

ALG14

N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase anchoring subunit ALG14, YBR070C
Component of UDP-GlcNAc transferase; required for the second step of dolichyl-linked oligosaccharide synthesis; anchors the catalytic subunit Alg13p to the ER membrane; similar to bacterial and human glycosyltransferases
Saccharomyces cerevisiae (S288c)

Affinity Capture-Western

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Publication

Hetero-oligomeric interactions between early glycosyltransferases of the dolichol cycle.

Noffz C, Keppler-Ross S, Dean N

N-Linked glycosylation begins with the formation of a dolichol-linked oligosaccharide in the endoplasmic reticulum (ER). The first two steps of this pathway lead to the formation of GlcNAc(2)-PP-dolichol, whose synthesis is sequentially catalyzed by the Alg7p GlcNAc phosphotransferase and by the dimeric Alg13p/Alg14p UDP-GlcNAc transferase on the cytosolic face of the endoplasmic reticulum. Here, we show that the Alg7p, Alg13p, ... [more]

Glycobiology May. 01, 2009; 19(5);472-8 [Pubmed: 19129246]

Throughput

  • Low Throughput

Curated By

  • BioGRID