Evidence map›Paper›PMID 1374414›Full record

ArticleThe Journal of cell biology1992

Specific association of the proto-oncogene product pp60c-src with an intracellular organelle, the PC12 synaptic vesicle.

A D Linstedt, M L Vetter, J M Bishop, R B Kelly

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Article
  3. Regulation of SRC family kinases in human cancers.Journal of signal transduction · 2011
    Article
  4. CD24 is expressed by myofiber synaptic nuclei and regulates synaptic transmission.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  5. Article
  6. Article
  7. Synaptophysin regulates activity-dependent synapse formation in cultured hippocampal neurons.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  8. A src family tyrosine kinase inhibits neurotransmitter release from neuronal cells.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Src interacts with dynamin and synapsin in neuronal cells.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  18. Synapsin I interacts with c-Src and stimulates its tyrosine kinase activity.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  19. Article
  20. Synaptophysin, a major synaptic vesicle protein, is not essential for neurotransmitter release.Proceedings of the National Academy of Sciences of the United States of America · 1996
    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

4 authors at 1 institution in 1 country.

A D LinstedtProgram in Neuroscience, University of California, San Francisco 94143-0534.
M L Vetter
J M Bishop
R B Kelly
University of California, San Francisco · US

Funding

ANTIBODIES TO SYNAPTIC VESICLESR01NS015927 · NINDS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI KELLY, REGIS B · 1985 to 2005
$1.5M
BIOCHEMISTRY OF SYNAPTIC TRANSMISSIONR01NS009878 · NINDS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI KELLY, REGIS B · 1985 to 2001
$574k
MEMBRANE TRAFFIC IN PEPTIDE HORMONE SECRETING CELLSR01DK033937 · NIDDK · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI KELLY, REGIS B · 1986 to 1995
–
NIDDK NIH HHS DK33937NINDS NIH HHS NS09878NINDS NIH HHS NS15927
6 · The paper itself

Abstract

The protein product of the proto-oncogene c-src is a membrane-associated tyrosine kinase of unknown function. Identification of pp60c-src target membranes may elucidate the function of the c-src protein. The available evidence indicates that pp60c-src associates with distinct membranes within single cell types and has different distributions in different cell types. Our experiments demonstrate targeting of pp60c-src to an isolatable and biochemically identified membrane fraction in the neuroendocrine cell line PC12. The c-src protein was found to be specifically associated with synaptic vesicles since: (a) the pp60c-src immunofluorescent pattern overlapped with a synaptic vesicle marker, synaptophysin; (b) a significant proportion (44%) of the pp60c-src from PC12 but not fibroblast postnuclear supernatants was recovered in a small vesicle fraction; (c) an anti-synaptophysin cytoplasmic domain antibody immunodepleted all of the pp60c-src vesicles in this fraction, and (d) pp60c-src copurified during a 100-fold purification of PC12 synaptic vesicles. These results suggest a role for the c-src protein in the regulation of synaptic vesicle function.

Indexed as

AnimalsFluorescent Antibody TechniqueImmunoblottingPC12 CellsProto-Oncogene Proteins pp60(c-src)Synaptic VesiclesSynaptophysinProto-Oncogene Proteins pp60(c-src)Synaptophysin

Identifiers

PMID1374414
PMCPMC2289481
OpenAlexW2147337689

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.