Evidence map›Paper›PMID 17898076›Full record

ArticleMolecular biology of the cell2007

Scd5p mediates phosphoregulation of actin and endocytosis by the type 1 phosphatase Glc7p in yeast.

Guisheng Zeng, Bo Huang, Suat Peng Neo, Junxia Wang, Mingjie Cai

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

15 citing papers in PubMed.

  1. Article
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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

5 authors.

Guisheng ZengInstitute of Molecular and Cell Biology, Singapore 138673, Republic of Singapore.
Bo Huang
Suat Peng Neo
Junxia Wang
Mingjie Cai

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pan1p plays essential roles in both actin and endocytosis in yeast. It interacts with, and regulates the function of, multiple endocytic proteins and actin assembly machinery. Phosphorylation of Pan1p by the kinase Prk1p down-regulates its activity, resulting in disassembly of the endocytic vesicle coat complex and termination of vesicle-associated actin polymerization. In this study, we focus on the mechanism that acts to release Pan1p from phosphorylation inhibition. We show that Pan1p is dephosphorylated by the phosphatase Glc7p, and the dephosphorylation is dependent on the Glc7p-targeting protein Scd5p, which itself is a phosphorylation target of Prk1p. Scd5p links Glc7p to Pan1p in two ways: directly by interacting with Pan1p and indirectly by interacting with the Pan1p-binding protein End3p. Depletion of Glc7p from the cells causes defects in cell growth, actin organization, and endocytosis, all of which can be partially suppressed by deletion of the PRK1 gene. These results suggest that Glc7p antagonizes the activity of the Prk1p kinase in regulating the functions of Pan1p and possibly other actin- and endocytosis-related proteins.

Indexed as

EndocytosisActinsCytoskeletal ProteinsFungal ProteinsGene DeletionGene Expression Regulation, FungalMicrofilament ProteinsMutationPhosphoprotein PhosphatasesPhosphorylationProtein BindingProtein Kinase CProtein Phosphatase 1Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsActinsCytoskeletal ProteinsEND3 protein, S cerevisiaeFungal ProteinsGLC7 protein, S cerevisiaeMicrofilament ProteinsPAN1 protein, S cerevisiaePhosphoprotein PhosphatasesProtein Kinase Cprotein kinase NProtein Phosphatase 1Saccharomyces cerevisiae ProteinsSCD5 protein, S cerevisiae

Identifiers

PMID17898076
PMCPMC2096580

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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.