Protein transport from the endoplasmic reticulum (ER) to the Golgi apparatus may be monitoredKeller, D SBaker, DHicke, LRexaeh, MSehleyer, MSchekman, RKabeenell, A K
Sorting membrane proteins by size in the Golgi De Caestecker and Macara find that the sorting of membrane proteins in the Golgi relies on a size filter that enables correct localization of proteins with a short cytosolic domain to the apical membrane. ...
Bos1p, a membrane protein required for ER to Golgi transport in yeast, co-purifies with the carrier vesicles and with Bet1p and the ER membrane. BOS1 and BET1 are required for transport from the ER to the Golgi complex in yeast and genetically interact with each other and a subset of ...
conventional protein secretion (CPS) is the trafficking route that secretory proteins undertake when are transported from the endoplasmic reticulum (ER) to the Golgi apparatus (GA), and subsequently to the plasma membrane (PM) via secretory vesicles...
What structures move proteins from the ER to the Golgi apparatus? Where does the Golgi apparatus send proteins? How are proteins packaged and transported within a cell? What is the role of Golgi apparatus in protein synthesis? How are proteins transported out of a cell? At the golgi it is...
By titrating wild-type and mutant apicoplast transit peptides against different ER retrieval sequences and studying protein transport in a brefeldin A-resistant parasite line, we generated data which suggest a direct involvement of the Golgi in traffic of soluble proteins to the P. falciparum ...
Nanjo Y, Oka H, Ikarashi N, Kaneko K, Kitajima A, Mitsui T, Muñoz FJ, Rodríguez-López M, Baroja-Fernández E, Pozueta-Romero J (2006) Rice plastidial N-glycosylated nucleotide pyrophosphatase/phosphodiesterase is transported from the ER-golgi to the chloroplast through the secretory pathwa...
1f). ERES are specialized ER domains that form transport carriers with protein cargoes destined for secretion via the Golgi apparatus53. Our screen identified most ERES proteins as required for GPAT4 targeting to LDs, including Sec12, Sec16, Tango1 and COPII coat components (Sar1, Sec23, Sec...
Most secreted and membrane proteins are co-translationally translocated across the SR/ER membrane, after which they are folded and further modified [25–27]. Properly folded proteins are then transported to the Golgi, where they are sorted to their final destinations; however, misfolded proteins ...
Recently, it was reported that the human INM protein Emerin is selectively cleared under ER stress through vesicular transport to lysosomes, but this process depends on Emerin’s LEM domain and is not observed for other INM proteins9. So far, we still miss key evidence to support the ...