Molecular recognition of cargo by the COPII complex: a most accommodating coat.
The molecular mechanism by which diverse cargo proteins are recognized and exported from the ER has been unclear. Two papers in this issue of Cell add clarity by mapping multiple cargo recognition sites in the Sec24 subunit of the COPII coat complex and demonstrating roles for these sites in export of specific protein cargos from the ER.
Barlowe
Charles
C
Dartmouth Medical School, Department of Biochemistry, Hanover, NH 03755, USA.
D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D010750:Phosphoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D021122:Protein Subunits / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D021381:Protein Transport / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D033921:Vesicular Transport Proteins
D002352:Carrier Proteins; D046911:Macromolecular Substances; D008565:Membrane Proteins; D010750:Phosphoproteins; D021122:Protein Subunits; C118289:SEC24 protein, S cerevisiae; C106113:SEC31 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D033921:Vesicular Transport Proteins