Evidence map›Paper›PMID 12006655›Full record

ArticleMolecular biology of the cell2002

t-SNARE phosphorylation regulates endocytosis in yeast.

Sangiliyandi Gurunathan, Michael Marash, Adina Weinberger, Jeffrey E Gerst

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.3field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 56 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Sangiliyandi GurunathanDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel.
Michael Marash
Adina Weinberger
Jeffrey E Gerst
Weizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Earlier we demonstrated that activation of a ceramide-activated protein phosphatase (CAPP) conferred normal growth and secretion to yeast lacking their complement of exocytic v-SNAREs (Snc1,2) or bearing a temperature-sensitive mutation in an exocytic t-SNARE (Sso2). CAPP activation led to Sso dephosphorylation and enhanced the assembly of t-SNAREs into functional complexes. Thus, exocytosis in yeast is modulated by t-SNARE phosphorylation. Here, we show that endocytic defects in cells lacking the v- and t-SNAREs involved in endocytosis are also rescued by CAPP activation. Yeast lacking the Tlg1 or Tlg2 t-SNAREs, the Snc v-SNAREs, or both, undergo endocytosis after phosphatase activation. CAPP activation correlated with restored uptake of FM4-64 to the vacuole, the uptake and degradation of the Ste2 receptor after mating factor treatment, and the dephosphorylation and assembly of Tlg1,2 into SNARE complexes. Activation of the phosphatase by treatment with C(2)-ceramide, VBM/ELO gene inactivation, or by the overexpression of SIT4 was sufficient to confer rescue. Finally, we found that mutation of single PKA sites in Tlg1 (Ser31 to Ala31) or Tlg2 (Ser90 to Ala90) was sufficient to restore endocytosis, but not exocytosis, to snc cells. These results suggest that endocytosis is also modulated by t-SNARE phosphorylation in vivo.

Indexed as

Membrane Transport ProteinsSaccharomyces cerevisiae ProteinsTranscription FactorsEndocytosisFungal ProteinsLigandsMacromolecular SubstancesMembrane ProteinsPhosphoprotein PhosphatasesPhosphorylationPhosphotransferasesPyridinium CompoundsQa-SNARE ProteinsQuaternary Ammonium CompoundsReceptors, Mating FactorReceptors, PeptideFM 4-64Fungal ProteinsLigandsMacromolecular SubstancesMembrane ProteinsMembrane Transport ProteinsN-acetylsphingosinePhosphoprotein PhosphatasesPhosphotransferasesPyridinium CompoundsQa-SNARE ProteinsQuaternary Ammonium CompoundsReceptors, Mating FactorReceptors, PeptideR-SNARE ProteinsSaccharomyces cerevisiae ProteinsSNC1 protein, S cerevisiaeSNC2 protein, S cerevisiaeSphingosineSSO2 protein, S cerevisiaeTLG2 protein, S cerevisiaeTranscription Factors

Identifiers

PMID12006655
PMCPMC111129
OpenAlexW2111524534

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.