Evidence map›Paper›PMID 10856229›Full record

ArticleThe EMBO journal2000

Increased protein kinase or decreased PP2A activity bypasses sphingoid base requirement in endocytosis.

S Friant, B Zanolari, H Riezman

Abstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
–field-weighted citation impact
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

47 citing papers in PubMed.

  1. Review
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  16. Article
  17. Article
  18. Distribution and functions of sterols and sphingolipids.Cold Spring Harbor perspectives in biology · 2011
    Review
  19. Article
  20. Review
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

3 authors.

S FriantBiozentrum of the University of Basel, CH-4056 Basel, Switzerland.
B Zanolari
H Riezman

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipids have been implicated in signal transduction and in several stages of membrane trafficking, but these two functions have not been functionally linked. In yeast, sphingoid base synthesis is required for the internalization step of endocytosis and organization of the actin cytoskeleton. We show that inactivation of a protein phosphatase 2A (PP2A) or overexpression of one of two kinases, Yck2p or Pkc1p, can specifically suppress the sphingoid base synthesis requirement for endocytosis. The two kinases have an overlapping function because only a mutant with impaired function of both kinases is defective in endocytosis. An ultimate target of sphingoid base synthesis may be the actin cytoskeleton, because overexpression of the kinases and inactivation of PP2A substantially corrected the actin defect due to the absence of sphingoid base. These results suggest that sphingoid base controls protein phosphorylation, perhaps by activating a signal transduction pathway that is required for endocytosis and proper actin cytoskeleton organization in yeast.

Indexed as

ActinsAcyltransferasesCasein KinasesCytoskeletonEndocytosisMutationPhosphoprotein PhosphatasesProtein Kinase CProtein KinasesProtein Phosphatase 2Saccharomyces cerevisiaeSerine C-PalmitoyltransferaseSignal TransductionSphingosineActinsAcyltransferasesCasein KinasesPhosphoprotein PhosphatasesProtein Kinase CProtein KinasesProtein Phosphatase 2Serine C-PalmitoyltransferaseSphingosine

Identifiers

PMID10856229
PMCPMC203374

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.