Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Chs7p, a new protein involved in the control of protein export from the endoplasmic reticulum that is specifically engaged in the regulation of chitin synthesis in Saccharomyces cerevisiae.
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Chs7 is an ER membrane protein required for Chs3 export from the ER and normal chitin synthase III activity.
"These results show that Chs7p forms part of a new mechanism specifically involved in Chs3p export from the ER and consequently, in the regulation of CSIII activity."
Specialized membrane-localized chaperones prevent aggregation of polytopic proteins in the ER.
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Chs7 belongs to a set of specialized ER membrane chaperones that keep their polytopic client proteins from aggregating during ER folding.
"In cells individually lacking one of these components only their cognate substrates, hexose transporters, phosphate transporters, and chitin synthase-III, respectively, aggregate and consequently fail to exit the ER membrane."
An in vivo map of the yeast protein interactome.
Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress.
A visual screen of protein localization during sporulation identifies new components of prospore membrane-associated complexes in budding yeast.
One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy.
The chaperone Chs7 forms a stable complex with Chs3 and promotes its activity at the cell surface.
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Chs7 remains associated with Chs3 beyond ER exit and can localize with Chs3 at the bud neck and other compartments.
"Here, we show that Chs7 itself exits the ER and localizes with Chs3 at the bud neck and intracellular compartments."
The social and structural architecture of the yeast protein interactome.
Multiple quality control mechanisms monitor yeast chitin synthase folding in the endoplasmic reticulum.
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Chs7 helps shield cytosolic Chs3 degrons from ERAD-C recognition.
"In addition, the interaction of Chs3 with its chaperone Chs7 seems to mask additional cytosolic degrons, thereby avoiding their recognition by the ERAD-C pathway."
Different Proteostasis Mechanisms Facilitate the Assembly of Individual Components on the Chitin Synthase 3 Complex at the Endoplasmic Reticulum.
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The 2025 Chs3/Chs7 trafficking study confirms Chs3-Chs7 complex assembly at the ER and focuses on quality control of orphan Chs7 and Chs3.
"Chitin synthase 3 complex assembly begins at the endoplasmic reticulum where the formation of a Chs3/Chs7 complex facilitates its exit from the ER and its transport along the secretory route."
Falcon deep research report for yeast CHS7
PANTHER PTHR35329 PAINT IBD annotations
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Current PTHR35329 PAINT places ER membrane, protein folding chaperone, chitin biosynthetic process, and protein folding on the fungal CHS7-family ancestor PTN002175570.
"PTHR35329 PTN002175570 GO:0044183 F IBD false SGD:S000001184 taxon:4751 20260611"
PANTHER family PTHR35329, Chitin synthase export chaperone