This is particularly true for the Golgi complex, which resides and functions at the crossroads of the secretory pathway. The Golgi receives newly synthesized proteins from the ER, covalently modifies them, and
Exit from the Golgi complex uses also a wide variety of signals (Fig. 1). These include signals to transport proteins to the endolysosomal compartment [9] and signals to transport proteins to the apical and basolateral domains of the plasma membrane [10]. Among the first group, the best-...
COG subunits, golgins, and Rabs were expressed as Gal4 binding or activation domain fusion proteins from pGAD/pGBD/pGBDU plamids (66). Rab binding domain fusion proteins contained mutations to lock the protein in the active (T) or inactive (D) conformation (67). Pairs of fusion constructs...
Endocytosed Shiga toxin is transported from the Golgi complex to the endoplasmic reticulum in butyric acid-treated A431 cells. We here examine the extent of this retrograde transport and its regulation. The short B fragment of Shiga toxin is sufficient for transport to the ER. The B fragment o...
After the exit of STING from the Golgi/TGN, STING translocates to recycling endosomes26,37. In line with this, colocalizations of mEos4b-STING with recycling endosomal proteins (transferrin receptor (TfnR) and Rab11) increased only 120-360 min after DMXAA stimulation (Fig. 3a−f). ...
Cholesterol biosynthesis is regulated by transcription factors SREBPs and their escort protein Scap. On sterol depletion, Scap/SREBP complex is transported from endoplasmic reticulum (ER) to the Golgi apparatus where SREBP is activated. Under cholesterol
Sec14 proteins are involved in the cytosolic transport of secretory proteins from the Golgi apparatus in yeast [30]. More recent research [31] indicates that Sec14 proteins are essential in membrane trafficking, connecting lipid metabolism with phosphoinositide signaling through transport of phosphatidylin...
ER and Golgi (Creemers2002; Gidalevitz et al.2013). Characteristic features of secreted proteins, such as biological activity, half-life time, or affinity to specific intracellular binding partners are modified by these events. The best-known example for a precursor protein (pro-protein) that un...
The GA receives proteins from the endoplasmic reticulum (ER) and modifies them through glycosylation, phosphorylation, and proteolytic cleavage. The GA also acts as a sorting center, packaging proteins into vesicles for transport to different cellular compartments, and ensures quality control by ...
Many diseases arise from genetic mutations that prevent synthesizing critical proteins. One such disease is Lowe disease (or oculocerebrorenal syndrome, because it affects the eyes, brain, and kidneys). In Lowe disease, there is a deficiency in an enzyme localized to the Golgi apparatus. Children...