Search results for "Vesicular-tubular cluster"
showing 3 items of 3 documents
Sorting signals in the cytosolic tail of plant p24 proteins involved in the interaction with the COPII coat.
2004
The ability of the cytosolic tail of a plant p24 protein to bind COPI and COPII subunits from plant and animal sources in vitro has been examined. We have found that a dihydrophobic motif in the -7,-8 position (relative to the cytosolic carboxy-terminus), which strongly cooperates with a dilysine motif in the -3,-4 position for COPI binding, is required for COPII binding. In addition, we show that COPI and COPII coat proteins from plant cytosol compete for binding to the sorting motifs in these tails. Only in the absence of the dilysine motif in the -3,-4 position or after COPI depletion could we observe COPII binding to the p24 tail. This competition is not observed when using rat liver cy…
Coupled transport of Arabidopsis p24 proteins at the ER–Golgi interface
2012
p24 proteins are a family of type I membrane proteins localized to compartments of the early secretory pathway and to coat protein I (COPI)- and COPII-coated vesicles. They can be classified, by sequence homology, into four subfamilies, named p24α, p24β, p24γ, and p24δ. In contrast to animals and fungi, plants contain only members of the p24β and p24δ subfamilies. It has previously been shown that transiently expressed red fluorescent protein (RFP)–p24δ5 localizes to the endoplasmic reticulum (ER) as a consequence of highly efficient COPI-based recycling from the Golgi apparatus. Using specific antibodies, endogenous p24δ5 has now been localized to the ER and p24β2 to the Golgi apparatus in…
Arabidopsis p24δ5 and p24δ9 facilitate Coat Protein I-dependent transport of the K/HDEL receptor ERD2 from the Golgi to the endoplasmic reticulum.
2014
The p24 proteins belong to a family of type I membrane proteins which cycle between the endoplasmic reticulum (ER) and Golgi via coat protein I (COPI) and COPII vesicles. Current nomenclature classifies them into four subfamilies, although plant p24 proteins belong to either the p24β or the p24δ subfamilies. Here, we show that Arabidopsis p24δ5/δ9 and HDEL ligands shift the steady-state distribution of the K/HDEL receptor ERD2 from the Golgi to the ER. We also show that p24δ5/δ9 interact directly with ERD2. This interaction requires the Golgi dynamics (GOLD) domain in p24δ5 and is much higher at acidic than at neutral pH, consistent with both proteins interacting at the cis-Golgi. In additi…