Evidence map›Paper›PMID 16166648›Full record

ArticleMolecular and cellular biology2005

Synaptotagmin VII is targeted to secretory organelles in PC12 cells, where it functions as a high-affinity calcium sensor.

Ping Wang, Michael C Chicka, Akhil Bhalla, David A Richards, Edwin R Chapman

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

43 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Lysosomal biogenesis and function in osteoclasts: a comprehensive review.Frontiers in cell and developmental biology · 2024
    Review
  3. Article
  4. Function of Drosophila Synaptotagmins in membrane trafficking at synapses.Cellular and molecular life sciences : CMLS · 2021
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Phosphatidylinositol 4,5-bisphosphate drives CaThe Journal of biological chemistry · 2019
    Article
  10. Distinct patterns of exocytosis elicited by CaPflugers Archiv : European journal of physiology · 2018
    Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

5 authors at 1 institution in 1 country.

Ping WangDepartment of Physiology, University of Wisconsin, 1300 University Ave., SMI 129, Madison, WI 53706, USA.
Michael C Chicka
Akhil Bhalla
David A Richards
Edwin R Chapman
University of Wisconsin–Madison · US

Funding

Synaptotagmin C2B Domain as a Ca2+ Sensing ModuleR01MH061876 · NIMH · UNIVERSITY OF WISCONSIN-MADISON · PI Edwin R Chapman · 2002 to 2026
$7.7M
SYNAPTOTAGMIN IN EXCITATION/SECRETION COUPLINGR01GM056827 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CHAPMAN, EDWIN R · 1998 to 2006
$1.8M
NIGMS NIH HHS GM 56827NIGMS NIH HHS R01 GM056827NIMH NIH HHS MH61876NIMH NIH HHS R01 MH061876
6 · The paper itself

Abstract

Synaptotagmin (syt) I is thought to act as a Ca2+ sensor that regulates neuronal exocytosis. Fifteen additional isoforms of syt have been identified, but their functions are less well understood. Here, we used PC12 cells to test the idea that different isoforms of syt impart cells with distinct metal (i.e., Ca2+, Ba2+, and Sr2+) requirements for secretion. These cells express syt's I and IX (syt IX sometimes referred to as syt V), which have low apparent metal affinities, at much higher levels than syt VII, which we show has a relatively high apparent affinity for metals. We found that syt I and VII partially colocalize on large dense core vesicles and that upregulation of syt VII produces a concomitant increase in the divalent cation sensitivity of catecholamine release from PC12 cells. Furthermore, RNA interference-mediated knockdown of endogenous syt VII reduced the metal sensitivity of release. These data support the hypothesis that the complement of syt's expressed by a cell, in conjunction with their metal affinity, determines the divalent cation sensitivity of exocytosis.

Indexed as

AnimalsBariumBase SequenceCalciumCatecholaminesCytoplasmDNA, ComplementaryDose-Response Relationship, DrugExocytosisGlutathione TransferaseImmunoblottingImmunohistochemistryLipidsLiposomesLysosomesMiceBariumCalciumCatecholaminesDNA, ComplementaryGlutathione TransferaseLipidsLiposomesOligonucleotidesProtein IsoformsRecombinant ProteinsStrontium

Identifiers

PMID16166648
PMCPMC1265757
OpenAlexW2153860862

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.