Evidence map›Paper›PMID 24990944›Full record

ReviewThe Journal of biological chemistry2014

Phospholipase D in cell signaling: from a myriad of cell functions to cancer growth and metastasis.

Julian Gomez-Cambronero

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
4.0field-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

49 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Genome-wide association studies ofInfection and immunity · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Microorganisms · 2022
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Identification and functional analysis of a novel phospholipase D2 gene mutation associated with familial systemic lupus erythematosus.Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2021
    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

1 author at 1 institution in 1 country.

Julian Gomez-CambroneroDepartment of Biochemistry and Molecular Biology, Boonshoft School of Medicine, Wright State University School of Medicine, Dayton, Ohio 45435. Electronic address: julian.cambronero@wright.edu.
Wright State University · US

Funding

PLD2, as a GEF or as a Lipase, is Central to Leukocyte ChemotaxisR01HL056653 · NHLBI · WRIGHT STATE UNIVERSITY · PI CAMBRONERO, JULIAN G. · 2004 to 2016
$4.0M
SIGNAL TRANSDUCTION IN NEUTROPHIL MEDIATED HEART INJURYR29HL056653 · NHLBI · WRIGHT STATE UNIVERSITY · PI GOMEZ-CAMBRONERO, JULIAN · 1998 to 2002
$301k
NHLBI NIH HHS HL056653-14NHLBI NIH HHS R01 HL056653NHLBI NIH HHS R29 HL056653
6 · The paper itself

Abstract

Phospholipase D (PLD) enzymes play a double vital role in cells: they maintain the integrity of cellular membranes and they participate in cell signaling including intracellular protein trafficking, cytoskeletal dynamics, cell migration, and cell proliferation. The particular involvement of PLD in cell migration is accomplished: (a) through the actions of its enzymatic product of reaction, phosphatidic acid, and its unique shape-binding role on membrane geometry; (b) through a particular guanine nucleotide exchange factor (GEF) activity (the first of its class assigned to a phospholipase) in the case of the mammalian isoform PLD2; and (c) through protein-protein interactions with a wide network of molecules: Wiskott-Aldrich syndrome protein (WASp), Grb2, ribosomal S6 kinase (S6K), and Rac2. Further, PLD interacts with a variety of kinases (PKC, FES, EGF receptor (EGFR), and JAK3) that are activated by it, or PLD becomes the target substrate. Out of these myriads of functions, PLD is becoming recognized as a major player in cell migration, cell invasion, and cancer metastasis. This is the story of the evolution of PLD from being involved in a large number of seemingly unrelated cellular functions to its most recent role in cancer signaling, a subfield that is expected to grow exponentially.

Indexed as

Cell MovementSignal TransductionAnimalsCell MembraneGRB2 Adaptor ProteinHumansNeoplasm MetastasisNeoplasm ProteinsNeoplasmsPhosphatidic AcidsPhospholipase DRAC2 GTP-Binding Proteinrac GTP-Binding ProteinsRibosomal Protein S6 KinasesWiskott-Aldrich Syndrome Protein FamilyGRB2 Adaptor ProteinGRB2 protein, humanNeoplasm ProteinsPhosphatidic AcidsPhospholipase Dphospholipase D2RAC2 GTP-Binding Proteinrac GTP-Binding ProteinsRibosomal Protein S6 KinasesWiskott-Aldrich Syndrome Protein FamilyCancer BiologyCell GrowthCell InvasionCell SignalingLipidLipid MetabolismMetastasisPhosphatidic Acid

Identifiers

PMID24990944
PMCPMC4132763
OpenAlexW2015708405

What Socratic 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 Socratic graph.