Akt phosphorylates Sec24: new clues into the regulation of ER-to-Golgi trafficking.
Regulation of protein transport within the early secretory pathway is a relatively unexplored area. Here, we propose a new player in the control of protein transport from the endoplasmic reticulum (ER) to the Golgi. Akt is an important signaling kinase whose functioning is perturbed in diseases such as cancer and diabetes. We discovered that Akt phosphorylates Sec24, an essential coat protein II (COPII) component involved in mediating cargo selection for ER-to-Golgi trafficking. We discuss how this finding may provide new insights into the regulation of protein transport.
BABS, School of Biotechnology and Biomolecular Sciences, Biosciences Building D26, University of New South Wales, Sydney, NSW 2052, Australia.
Laura J
LJ
Sharpe
Winnie
W
Luu
Andrew J
AJ
Brown
D000818:Animals; D016466:CHO Cells; D006224:Cricetinae; D003412:Cricetulus; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006056:Golgi Apparatus / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D051379:Mice; D010766:Phosphorylation; D051057:Proto-Oncogene Proteins c-akt / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D033921:Vesicular Transport Proteins / Q000235:genetics / Q000378:metabolism*
D011994:Recombinant Proteins; C530638:SEC24A protein, human; D033921:Vesicular Transport Proteins; D051057:Proto-Oncogene Proteins c-akt