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
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
A role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiae.
Cytoplasm to vacuole trafficking of aminopeptidase I requires a t-SNARE-Sec1p complex composed of Tlg2p and Vps45p.
Pep3p/Pep5p complex: a putative docking factor at multiple steps of vesicular transport to the vacuole of Saccharomyces cerevisiae.
Vps45p stabilizes the syntaxin homologue Tlg2p and positively regulates SNARE complex formation.
A novel phospholipid-binding protein from the yeast Saccharomyces cerevisiae with dual binding specificities for the transport GTPase Ypt7p and the Sec1-related Vps33p.
Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants.
Proteome survey reveals modularity of the yeast cell machinery.
The Sec1p/Munc18 protein Vps45p binds its cognate SNARE proteins via two distinct modes.
High-quality binary protein interaction map of the yeast interactome network.
The N-terminal peptide of the syntaxin Tlg2p modulates binding of its closed conformation to Vps45p.
An inter-species protein-protein interaction network across vast evolutionary distance.
The social and structural architecture of the yeast protein interactome.
STT10, a novel class-D VPS yeast gene required for osmotic integrity related to the PKC1/STT1 protein kinase pathway.
Yeast Vps45p is a Sec1p-like protein required for the consumption of vacuole-targeted, post-Golgi transport vesicles.
Genetic interactions between a pep7 mutation and the PEP12 and VPS45 genes: evidence for a novel SNARE component in transport between the Saccharomyces cerevisiae Golgi complex and endosome.
The vesicle transport protein Vps33p is an ATP-binding protein that localizes to the cytosol in an energy-dependent manner.
Traffic into the prevacuolar/endosomal compartment of Saccharomyces cerevisiae: a VPS45-dependent intracellular route and a VPS45-independent, endocytic route.
Falcon deep research report for Saccharomyces cerevisiae VPS45 (P38932; YGL095C)
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Vps45p is an endosomal Sec1/Munc18 (SM) family protein that binds the cognate syntaxin t-SNAREs Tlg2p and Pep12p, forming distinct Vps45p-Tlg2p and Vps45p-Pep12p complexes.
"physically associates with the syntaxin-like t-SNARE **Tlg2p** and also forms a separate complex with the endosomal t-SNARE **Pep12p**; co-immunoprecipitation data support **distinct Vps45p–Tlg2p and Vps45p–Pep12p complexes**"
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Vps45p positively regulates productive SNARE complex assembly; loss of VPS45 prevents Tlg2p from pairing with its cognate partners Tlg1p and Vti1p.
"Deletion of **VPS45** causes loss of functional Tlg2-dependent SNARE pairing: even when Tlg2 is stabilized, it fails to bind cognate partners **Tlg1p and Vti1p**, indicating Vps45p is required for productive SNARE complex formation"
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Vps45p stabilizes the syntaxin Tlg2p, protecting it from rapid proteasome-dependent degradation; stabilized Tlg2p localizes correctly but remains non-functional for SNARE assembly without Vps45p.
"Vps45p stabilizes Tlg2p: in **vps45Δ**, Tlg2p is lost through **rapid proteasomal down-regulation**, and proteasome impairment (but not loss of vacuolar proteases) restores Tlg2p levels"
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Vps45p defines a VPS45-dependent intracellular (biosynthetic) route from the Golgi/TGN to the prevacuolar compartment, distinct from a VPS45-independent endocytic route from the plasma membrane to the PVC.
"A **VPS45-independent endocytic route** (plasma membrane → PVC), demonstrated by delivery of endocytosed cargo (e.g., Ste3p) to the PVC without VPS45 function"
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Vps45p and Tlg2p are required for the constitutive cytoplasm-to-vacuole targeting (Cvt) pathway of aminopeptidase I, but are dispensable for starvation-induced macroautophagy.
"Vps45p and Tlg2p are required for maturation/processing of API via the constitutive Cvt route: **vps45ts** mutants fail to mature API at non-permissive temperature, phenocopying **tlg2Δ**"
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Vps45p is recruited to endosomal docking/fusion sites by the Vac1p adaptor, which integrates Vps21p (Rab5-like) GTPase activity and Vps34-generated PI(3)P.
"Vac1p **co-precipitates Vps45p**; this interaction persists without Pep12p, supporting a direct or Pep12-independent association"
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Vps45p is predominantly membrane-associated in wild-type cells in a Tlg2-dependent manner, becoming more cytosolic when the Tlg2 N-terminal Vps45-binding region is removed; it cycles on and off membranes.
"Vps45p is membrane-associated when full-length Tlg2p is present, but becomes more **cytosolic** when Tlg2 lacks its N-terminal Vps45-binding region (Δ1–230)"
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Modern consensus frames SM proteins, including the endosomal SM Vps45, as active chaperones that template productive trans-SNARE complex assembly rather than passive syntaxin binders.
"Modern consensus frames SM proteins as **active chaperones for productive trans-SNARE complex assembly**, rather than passive syntaxin binders"
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Quantitatively, vps45 loss causes strong CPY mis-sorting (~70% CPY secretion vs ~2-4% in wild type), underscoring its central role in vacuolar protein sorting.
"In yeast, vps45Δ causes strong CPY mis-sorting, with **~70% CPY secretion** versus **~2–4%** in wild type"