Evidence map›Paper›PMID 35231723›Full record

ReviewAdvances in biological regulation2022

Phosphorylation-mediated regulation of the Nem1-Spo7/Pah1 phosphatase cascade in yeast lipid synthesis.

Shoily Khondker, Gil-Soo Han, George M Carman

Open access · greenAbstract readReview
In one paragraph

Review in Advances in biological regulation, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.8field-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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Architecture and function of yeast phosphatidate phosphatase Pah1 domains/regions.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. 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 at 1 institution in 1 country.

Shoily KhondkerDepartment of Food Science and the Rutgers Center for Lipid Research, New Jersey Institute for Food, Nutrition, and Health, Rutgers University, New Brunswick, NJ, 08901, USA.
Gil-Soo HanDepartment of Food Science and the Rutgers Center for Lipid Research, New Jersey Institute for Food, Nutrition, and Health, Rutgers University, New Brunswick, NJ, 08901, USA.
George M CarmanDepartment of Food Science and the Rutgers Center for Lipid Research, New Jersey Institute for Food, Nutrition, and Health, Rutgers University, New Brunswick, NJ, 08901, USA. Electronic address: gcarman@rutgers.edu.
Rutgers, The State University of New Jersey · US

Funding

REGULATION OF PHOSPHOLIPID SYNTHESIS BY CTPR01GM050679 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI CARMAN, GEORGE M. · 1994 to 2019
$6.0M
Regulation and Role of Phosphatidate Phosphatase in Lipid MetabolismR35GM136128 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI GEORGE M. CARMAN · 2020 to 2026
$4.1M
Phospholipid metabolism and membrane functionR37GM028140 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI CARMAN, GEORGE M. · 2010 to 2019
$4.0M
PHOSPHOLIPID METABOLSIM AND MEMBRANE FUNCTIONR01GM028140 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI CARMAN, GEORGE M. · 1985 to 2009
$3.2M
NIGMS NIH HHS R01 GM028140NIGMS NIH HHS R01 GM050679NIGMS NIH HHS R35 GM136128NIGMS NIH HHS R37 GM028140
6 · The paper itself

Abstract

The PAH1-encoded phosphatidate phosphatase, which catalyzes the dephosphorylation of phosphatidate to produce diacylglycerol, controls the divergence of phosphatidate into triacylglycerol synthesis and phospholipid synthesis. Pah1 is inactive in the cytosol as a phosphorylated form and becomes active on the nuclear/endoplasmic reticulum membrane as a dephosphorylated form by the Nem1-Spo7 protein phosphatase complex. The phosphorylation of Pah1 by protein kinases, which include casein kinases I and II, Pho85-Pho80, Cdc28-cyclin B, and protein kinases A and C, controls its cellular location, catalytic activity, and susceptibility to proteasomal degradation. Nem1 (catalytic subunit) and Spo7 (regulatory subunit), which form a protein phosphatase complex catalyzing the dephosphorylation of Pah1 for its activation, are phosphorylated by protein kinases A and C. In this review, we discuss the functions and interrelationships of the protein kinases in the control of the Nem1-Spo7/Pah1 phosphatase cascade and lipid synthesis.

Indexed as

LipidsMembrane ProteinsNuclear ProteinsPhosphatidate PhosphataseSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsPhosphorylationProtein KinasesLipidsMembrane ProteinsNem1 protein, S cerevisiaeNuclear ProteinsPAH1 protein, S cerevisiaePhosphatidate PhosphataseProtein KinasesSaccharomyces cerevisiae ProteinsSPO7 protein, S cerevisiaeDiacylglycerolNem1-Spo7 protein phosphatasePah1 PA phosphatasePhosphatidic acidPhospholipidProtein kinaseTriacylglycerolYeast

Identifiers

PMID35231723
PMCPMC9149063
OpenAlexW4213456551

What OpenQuestion holds

Textmetadata
LicenceTDM
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.