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Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes
TLDR
The mammalian homologue of Atg9p, a multi-spanning transmembrane protein essential in yeast for autophagy, is studied to gain a better understanding of the function of this ubiquitious protein. Expand
An alternative protein targeting pathway in Escherichia coli: studies on the role of FtsY.
TLDR
Observations suggest that FtsY is the functional E. coli homolog of the mammalianSRP receptor, which shares sequence similarity with the alpha‐subunit of the eukaryotic SRP receptor (‘docking protein’) in the membrane of the endoplasmic reticulum. Expand
The Escherichia coli SRP and SecB targeting pathways converge at the translocon
TLDR
It is demonstrated here that the SRP pathway delivers nascent inner membrane proteins at the membrane through a protein cross‐linking approach that delivers a variety of precursor proteins to a common membrane translocation complex of the E. coli inner membrane. Expand
ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin.
TLDR
It is proposed that ERp57 forms complexes with both calnexin and calreticulin and propose that it is these complexes that can specifically modulate glycoprotein folding within the ER lumen. Expand
Interaction of the Thiol-Dependent Reductase ERp57 with Nascent Glycoproteins
TLDR
It is likely that ERp57 functions as part of the glycoprotein-specific quality control machinery operating in the lumen of the ER. Expand
Signal recognition particle mediates post‐translational targeting in eukaryotes
TLDR
It is shown that SRP can associate post‐translationally with this type of ER‐targeting signal, and deliver newly synthesised TA proteins to the ER membrane by a pathway dependent upon GTP and the SRP receptor, and it is found that dependency upon this SRP‐dependent route is precursor specific. Expand
Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides.
TLDR
Cross‐linking is used to demonstrate that E. coli SRP interacts with a variety of nascent presecretory proteins and integral inner membrane proteins, and proposes that SRP and trigger factor act as secretion‐specific and general molecular chaperone respectively, early in protein synthesis. Expand
Post-translational integration of tail-anchored proteins is facilitated by defined molecular chaperones
TLDR
This study reconstituted the membrane integration of TA proteins using purified components and finds that a combination of Hsc70 and Hsp40 can completely substitute for the ATP-dependent factors present in cytosol. Expand
A Precursor-specific Role for Hsp40/Hsc70 during Tail-anchored Protein Integration at the Endoplasmic Reticulum*
TLDR
The hydrophobicity of the TA region dictates whether a precursor is delivered to the ER via the Hsp40/Hsc70 or Asna-1/TRC40-dependent route, and it is concluded that these distinct cytosolic ATPases are responsible for two different ATP-dependent pathways of TA protein biogenesis. Expand
Bat3 promotes the membrane integration of tail-anchored proteins
TLDR
It is proposed that Bat3 either modulates the TRC40 pathway in higher eukaryotes or provides an alternative fate for newly synthesised tail-anchored proteins. Expand
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