Evidence map›Paper›PMID 7565716›Full record

ArticleMolecular and cellular biology1995

A phosphatidylinositol (PI) kinase gene family in Dictyostelium discoideum: biological roles of putative mammalian p110 and yeast Vps34p PI 3-kinase homologs during growth and development.

K Zhou, K Takegawa, S D Emr, R A Firtel

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In one paragraph

Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

46 citing papers in PubMed, 126 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Function of small GTPases in Dictyostelium macropinocytosis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. PI3K signalling: the path to discovery and understanding.Nature reviews. Molecular cell biology · 2012
    Article
  11. Article
  12. PI3K: from the bench to the clinic and back.Current topics in microbiology and immunology · 2010
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
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.

K ZhouDepartment of Biology, Howard Hughes Medical Institute, University of California, San Diego, La Jolla 92093-0634, USA.
K Takegawa
S D Emr
R A Firtel
Howard Hughes Medical Institute · US

Funding

STRUCTURE/FUNCTION STUDY OF CDC34K08CA060559 · NCI · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI STEUSSY, CALVIN N · 1995 to 1997
–
NCI NIH HHS CA60559
6 · The paper itself

Abstract

Three groups of phosphatidylinositol (PI) kinases convert PI into PI(3)phosphate, PI(4)phosphate, PI(4,5) bisphosphate, and PI(3,4,5)trisphosphate. These phosphoinositides have been shown to function in vesicle-mediated protein sorting, and they serve as second-messenger signaling molecules for regulating cell growth. To further elucidate the mechanism of regulation and function of phosphoinositides, we cloned genes encoding five putative PI kinases from Dictyostelium discoideum. Database analysis indicates that D. discoideum PIK1 (DdPIK1), -2, and -3 are most closely related to the mammalian p110 PI 3-kinase, DdPIK5 is closest to the yeast Vps34p PI 3-kinase, and DdPIK4 is most homologous to PI 4-kinases. Together with other known PI kinases, a superfamily of PI kinase genes has been defined, with all of the encoded proteins sharing a common highly conserved catalytic core domain. DdPIK1, -2, and -3 may have redundant functions because disruption of any single gene had no effect on D. discoideum growth or development. However, strains in which both of the two most highly related genes, DdPIK1 and DdPIK2, were disrupted showed both growth and developmental defects, while double knockouts of DdPIK1 and DdPIK3 and DdPIK2 and DdPIK3 appear to be lethal. The delta Ddpik1 delta Ddpik2 null cells were smaller than wild-type cells and grew slowly both in association with bacteria and in axenic medium when attached to petri plates but were unable to grow in suspension in axenic medium. When delta Ddpik1 delta Ddpik2 null cells were plated for multicellular development, they formed aggregates having multiple tips and produced abnormal fruiting bodies. Antisense expression of DdPIK5 (a putative homolog of the Saccharomyces cerevisiae VPS34) led to a defect in the growth of D. discoideum cells on bacterial lawns and abnormal development. DdPIK5 complemented the temperature-sensitive growth defect of a Schizosaccharomyces pombe delta Svps34 mutant strain, suggesting DdPIK5 encodes a functional homolog of yeast Vps34p. These observations indicate that in D. discoideum, different PI kinases regulate distinct cellular processes, including cell growth, development, and protein trafficking.

Indexed as

Saccharomyces cerevisiae Proteins1-Phosphatidylinositol 4-KinaseAmino Acid SequenceAnimalsBase SequenceCloning, MolecularConserved SequenceDictyosteliumGene Expression Regulation, DevelopmentalGene Expression Regulation, FungalGenes, FungalMammalsMolecular Sequence DataMultigene FamilyPhosphatidylinositol 3-KinasesPhosphotransferases (Alcohol Group Acceptor)1-Phosphatidylinositol 4-KinasePhosphatidylinositol 3-KinasesPhosphotransferases (Alcohol Group Acceptor)PIK1 protein, S cerevisiaeRNA, AntisenseSaccharomyces cerevisiae Proteins

Identifiers

PMID7565716
PMCPMC230815
OpenAlexW2104834552

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.