Evidence map›Paper›PMID 11050165›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Peripheral Golgi protein GRASP65 is a target of mitotic polo-like kinase (Plk) and Cdc2.

C Y Lin, M L Madsen, F R Yarm, Y J Jang, X Liu, R L Erikson

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
–field-weighted citation impact
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

60 citing papers in PubMed.

  1. Golgi defect as a major contributor to lysosomal dysfunction.Frontiers in cell and developmental biology · 2024
    Review
  2. Article
  3. Article
  4. Adaptation of the Golgi Apparatus in Cancer Cell Invasion and Metastasis.Frontiers in cell and developmental biology · 2021
    Review
  5. Article
  6. Membrane and organelle dynamics during cell division.Nature reviews. Molecular cell biology · 2020
    Review
  7. Article
  8. Unlocking Golgi: Why Does Morphology Matter?Biochemistry. Biokhimiia · 2019
    Review
  9. Article
  10. Golgi Structure and Function in Health, Stress, and Diseases.Results and problems in cell differentiation · 2019
    Review
  11. Article
  12. Article
  13. Article
  14. GRASP: A Multitasking Tether.Frontiers in cell and developmental biology · 2016
    Review
  15. Article
  16. Mechanisms and Regulation of the Mitotic Inheritance of the Golgi Complex.Frontiers in cell and developmental biology · 2015
    Review
  17. Article
  18. Article
  19. Aβ-induced Golgi fragmentation in Alzheimer's disease enhances Aβ production.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

6 authors.

C Y LinDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA. chin-yo_lin@student.hms.harvard.edu
M L Madsen
F R Yarm
Y J Jang
X Liu
R L Erikson

Funding

BIOCHEMISTRY OF THE CANCER CELLR35CA042580 · NCI · HARVARD UNIVERSITY · PI ERIKSON, RAYMOND L · 1986 to 1999
–
NCI NIH HHS CA42580
6 · The paper itself

Abstract

Cell division is characterized by orchestrated events of chromosome segregation, distribution of cellular organelles, and the eventual partitioning and separation of the two daughter cells. Mitotic kinases, including polo-like kinases (Plk), influence multiple events in mitosis. In yeast two-hybrid screens using mammalian Plk C-terminal domain baits, we have identified Golgi peripheral protein GRASP65 (Golgi reassembly stacking protein of 65 kDa) as a Plk-binding protein. GRASP65 appears to function in the postmitotic reassembly of Golgi stacks. In this report we demonstrate binding between Plk and GRASP65 and provide in vitro and in vivo evidence that Plk is a GRASP65 kinase. Moreover, we show that Cdc2 can also phosphorylate GRASP65. In addition, we present data which support the observation that the conserved C terminus of Plk is important for its function. Deletion or frameshift mutations in the conserved C-terminal domain of Plk greatly diminish its ability to phosphorylate GRASP65. These and previous findings suggest that phosphorylation of Golgi components by mitotic kinases may regulate mechanisms of Golgi inheritance during cell division.

Indexed as

Cell Cycle ProteinsSaccharomyces cerevisiae ProteinsAnimalsCDC2 Protein KinaseCell LineCOS CellsFungal ProteinsGene ExpressionGolgi ApparatusGolgi Matrix ProteinsMembrane ProteinsMitosisMutagenesisOligopeptidesPeptidesPhosphorylationCDC2 Protein KinaseCDC5 protein, S cerevisiaeCell Cycle ProteinsFLAG peptideFungal ProteinsGolgi Matrix ProteinsGORASP1 protein, humanMembrane ProteinsOligopeptidesPeptidesProtein KinasesProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID11050165
PMCPMC18808

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.