Differential requirements for ts-O45-G and procollagen biosynthetic transport.
Emerging experimental evidence favours the existence of cargo sorting occurring upon the endoplasmic reticulum (ER) exit. Recent studies revealed that, in contrast to the conventional secretory marker ts-O45-G, procollagen (PC I) exits the ER at sites not coated with coat protein II and is transported to the Golgi complex in carriers devoid of coat protein I. Here, we investigated whether PC I trafficking requires a different molecular machinery in comparison with the ts-O45-G. By combining colocalization of the cargoes with endogenous markers, downregulation of transport machinery by RNA interference and knock-ins by complementary DNA over-expression, we provide strong evidence that PC I and ts-O45-G have common but also different molecular requirements during pre- and post-Golgi trafficking events.
Starkuviene
Vytaute
V
Cell Biology and Cell Biophysics Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany. starkuvi@embl-heidelberg.de
Pepperkok
Rainer
R
D000818:Animals; D020755:Coat Protein Complex I / Q000502:physiology*; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006056:Golgi Apparatus / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000378:metabolism*; D051379:Mice; D041681:NIH 3T3 Cells; D011347:Procollagen / Q000378:metabolism*; D014759:Viral Envelope Proteins / Q000378:metabolism*
D020755:Coat Protein Complex I; C028391:G protein, vesicular stomatitis virus; D008562:Membrane Glycoproteins; D011347:Procollagen; D014759:Viral Envelope Proteins