Evidence map›Paper›PMID 10888662›Full record

ArticleMolecular biology of the cell2000

Accumulation of rab4GTP in the cytoplasm and association with the peptidyl-prolyl isomerase pin1 during mitosis.

L Gerez, K Mohrmann, M van Raak, M Jongeneelen, X Z Zhou, K P Lu, P van Der Sluijs

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

14 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Small RAB GTPases Regulate Multiple Steps of Mitosis.Frontiers in cell and developmental biology · 2016
    Review
  3. Article
  4. Article
  5. Protein kinase Cδ differentially regulates cAMP-dependent translocation of NTCP and MRP2 to the plasma membrane.American journal of physiology. Gastrointestinal and liver physiology · 2012
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  14. 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

7 authors at 3 institutions in 2 countries.

L GerezDepartment of Cell Biology and Institute of Biomembranes, Utrecht University Medical Center, 3584 CX Utrecht, The Netherlands.
K Mohrmann
M van Raak
M Jongeneelen
X Z Zhou
K P Lu
P van Der Sluijs
Utrecht University · NLBeth Israel Deaconess Medical Center · USHarvard University · US

Funding

Function and Regulation of the Prolyl Isomerase Pin1R01GM058556 · NIGMS · BETH ISRAEL DEACONESS MEDICAL CENTER · PI LU, KUN PING · 1999 to 2010
$3.9M
Function and Regulation of Pin2/TRF1 and PinX1R01GM056230 · NIGMS · BETH ISRAEL DEACONESS MEDICAL CENTER · PI LU, KUN PING · 1997 to 2005
$1.8M
NIGMS NIH HHS R01 GM056230NIGMS NIH HHS R01 GM058556NIGMS NIH HHS R01GM56230NIGMS NIH HHS R01GM58556
6 · The paper itself

Abstract

Transport through the endocytic pathway is inhibited during mitosis. The mechanism responsible for this inhibition is not understood. Rab4 might be one of the proteins involved as it regulates transport through early endosomes, is phosphorylated by p34(cdc2) kinase, and is translocated from early endosomes to the cytoplasm during mitosis. We investigated the perturbation of the rab4 GTPase cycle during mitosis. Newly synthesized rab4 was less efficiently targeted to membranes during mitosis. By subcellular fractionation of mitotic cells, we found a large increase of cytosolic rab4 in the active GTP-form, an increase not associated with the cytosolic rabGDP chaperone GDI. Instead, phosphorylated rab4 is in a complex with the peptidyl-prolyl isomerase Pin1 during mitosis, but not during interphase. Our results show that less efficient recruitment of rab4 to membranes and a bypass of the normal GDI-mediated retrieval of rab4GDP from early endosomes reduce the amount of rab4GTP on membranes during mitosis. We propose that phosphorylation of rab4 inhibits both the recruitment of rab4 effector proteins to early endosomes and the docking of rab4-containing transport vesicles. This mechanism might contribute to the inhibition of endocytic membrane transport during mitosis.

Indexed as

AnimalsBiological TransportCHO CellsCricetinaeCytoplasmGuanine Nucleotide Dissociation InhibitorsGuanosine DiphosphateGuanosine TriphosphateIntracellular MembranesMitosisNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePhosphorylationrab4 GTP-Binding ProteinsGDP dissociation inhibitor 1Guanine Nucleotide Dissociation InhibitorsGuanosine DiphosphateGuanosine TriphosphateNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl Isomeraserab4 GTP-Binding Proteins

Identifiers

PMID10888662
PMCPMC14913
OpenAlexW2110522985

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.