Evidence map›Paper›PMID 22991193›Full record

ArticleJournal of lipid research2012

Phosphatidic acid regulation of PIPKI is critical for actin cytoskeletal reorganization.

Akua N Roach, Ziqing Wang, Ping Wu, Feng Zhang, Robin B Chan, Yoshiya Yonekubo, Gilbert Di Paolo, Alemayehu A Gorfe, Guangwei Du

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2012. 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
2.0field-weighted citation impact, top 15% 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, 49 citations in OpenAlex.

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  8. Phosphatidic acid generated by PLD2 promotes the plasma membrane recruitment of IQGAP1 and neointima formation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
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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

9 authors at 3 institutions in 1 country.

Akua N RoachDepartment of Pharmacology and Center for Developmental Genetics, Stony Brook University, Stony Brook, NY 11794, USA.
Ziqing Wang
Ping Wu
Feng Zhang
Robin B Chan
Yoshiya Yonekubo
Gilbert Di Paolo
Alemayehu A Gorfe
Guangwei Du
The University of Texas Health Science Center at Houston · USColumbia University Irving Medical Center · USStony Brook University · US

Funding

Role of phospholipids in membrane traffic at the synapseR01NS056049 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI LIEM, RONALD K. · 2006 to 2016
$3.7M
Roles of Phospholipase D in AT1 Receptor EndocytosisR01GM071475 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI DU, GUANGWEI · 2006 to 2010
$1.6M
NIGMS NIH HHS GM-071475NIGMS NIH HHS R01 GM071475NINDS NIH HHS NS-056049NINDS NIH HHS R01 NS056049
6 · The paper itself

Abstract

Type I phosphatidylinositol-4-phosphate 5-kinase (PIPKI) is the main enzyme generating the lipid second messenger phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2], which has critical functions in many cellular processes, such as cytoskeletal reorganization, membrane trafficking, and signal transduction. All three members of the PIPKI family are activated by phosphatidic acid (PA). However, how PA regulates the activity and functions of PIPKI have not been fully elucidated. In this study, we identify a PA-binding site on PIPKIγ. Mutation of this site inhibited the PA-stimulated activity and membrane localization of PIPKIγ as well as the formation of actin comets and foci induced by PIPKIγ. We also demonstrate that phospholipase D (PLD) generates a pool of PA involved in PIPKIγ regulation by showing that PLD inhibitors blocked the membrane localization of PIPKIγ and its ability to induce actin cytoskeletal reorganization. Targeting the PIPKIγ PA-binding-deficient mutant to membranes by a membrane localization sequence failed to restore the actin reorganization activity of PIPKIγ, suggesting that PA binding is not only involved in recruiting PIPKIγ to membranes but also may induce a conformational change. Taken together, these results reveal a new molecular mechanism through which PA regulates PIPKI and provides direct evidence that PA is important for the localization and functions of PIPKI in intact cells.

Indexed as

ActinsAnimalsBinding SitesCells, CulturedChlorocebus aethiopsCOS CellsCytoskeletonEnzyme InhibitorsModels, MolecularMutationPhosphatidic AcidsPhospholipase DPhosphotransferases (Alcohol Group Acceptor)Recombinant ProteinsSequence Analysis, DNAStructure-Activity Relationship1-phosphatidylinositol-4-phosphate 5-kinaseActinsEnzyme InhibitorsPhosphatidic AcidsPhospholipase DPhosphotransferases (Alcohol Group Acceptor)Recombinant Proteins

Identifiers

PMID22991193
PMCPMC3494241
OpenAlexW2162316048

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.