R. Hegde

Publications197
h-index69
Citations12,510
Highly Influential Citations846
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Identification of a Targeting Factor for Posttranslational Membrane Protein Insertion into the ER
View on Elsevier
A transmembrane form of the prion protein in neurodegenerative disease.
TLDR
Aberrant regulation of protein biogenesis and topology at the endoplasmic reticulum can result in neurodegeneration.
View on PubMed
Formation of stacked ER cisternae by low affinity protein interactions
TLDR
Results point to a molecular mechanism for OSER biogenesis that involves weak homotypic interactions between cytoplasmic domains of proteins, which may underlie the formation of other stacked membrane structures within cells.
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A Ribosome-Associating Factor Chaperones Tail-Anchored Membrane Proteins
TLDR
The Bat3 complex acts as a TMD-selective chaperone that effectively channels TA proteins to the TRC40 insertion pathway, explaining their mislocalization in the analogous yeast deletion strains.
View on Nature
Protein Targeting and Degradation are Coupled for Elimination of Mislocalized Proteins
TLDR
It is found that nascent membrane proteins tethered to ribosomes are not substrates for ubiquitination unless they are released into the cytosol, and it is proposed that such coupling allows the fast tracking of MLPs for degradation without futile engagement of the cytOSolic folding machinery.
View on Nature
ZNF598 Is a Quality Control Sensor of Collided Ribosomes
View on PubMed
Structural basis for stop codon recognition in eukaryotes
TLDR
Cryo-electron microscopy structures at 3.5–3.8 Å resolution are presented, providing a molecular framework for eukaryotic stop codon recognition and have implications for future studies on the mechanisms of canonical and premature translation termination.
View on Nature
A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation.
View on PubMed
Regulation of basal cellular physiology by the homeostatic unfolded protein response
TLDR
Findings are revealing that the UPR causally contributes to disease not just by its role in protein folding but also through its broad influence on cellular physiology.
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The role of p58IPK in protecting the stressed endoplasmic reticulum.
TLDR
A previously unanticipated location for p58(IPK) in the ER lumen is identified where its putative function as a cochaperone explains the stress-sensitivity phenotype of knockout cells and mice.
View on PubMed
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