PMID- 10468580
OWN - NLM
STAT- MEDLINE
DCOM- 19991007
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 18
DP  - 1999 Aug 31
TI  - Syntaxin 1 interacts with the L(D) subtype of voltage-gated Ca(2+) channels in
      pancreatic beta cells.
PG  - 10164-9
AB  - Interaction of syntaxin 1 with the alpha(1D) subunit of the voltage-gated L type 
      Ca(2+) channel was investigated in the pancreatic beta cell. Coexpression of the 
      enhanced green fluorescent protein-linked alpha(1D) subunit with the enhanced
      blue fluorescent protein-linked syntaxin 1 and Western blot analysis together
      with subcellular fractionation demonstrated that the alpha(1D) subunit and
      syntaxin 1 were colocalized in the plasma membrane. Furthermore, the alpha(1D)
      subunit was coimmunoprecipitated efficiently by a polyclonal antibody against
      syntaxin 1. Syntaxin 1 also played a central role in the modulation of L type
      Ca(2+) channel activity because there was a faster Ca(2+) current run-down in
      cells incubated with antisyntaxin 1 compared with controls. In parallel,
      antisyntaxin 1 markedly reduced insulin release in both intact and permeabilized 
      cells, subsequent to depolarization with K(+) or exposure to high Ca(2+).
      Exchanging Ca(2+) for Ba(2+) abolished the effect of antisyntaxin 1 on both
      Ca(2+) channel activity and insulin exocytosis. Moreover, antisyntaxin 1 had no
      significant effects on Ca(2+)-independent insulin release trigged by hypertonic
      stimulation. This suggests that there is a structure-function relationship
      between the alpha(1D) subunit of the L type Ca(2+) channel and the exocytotic
      machinery in the pancreatic beta cell.
FAU - Yang, S N
AU  - Yang SN
AD  - The Rolf Luft Center for Diabetes Research, Department of Molecular Medicine,
      Karolinska Institutet, Karolinska Hospital, S-171 76 Stockholm, Sweden.
FAU - Larsson, O
AU  - Larsson O
FAU - Branstrom, R
AU  - Branstrom R
FAU - Bertorello, A M
AU  - Bertorello AM
FAU - Leibiger, B
AU  - Leibiger B
FAU - Leibiger, I B
AU  - Leibiger IB
FAU - Moede, T
AU  - Moede T
FAU - Kohler, M
AU  - Kohler M
FAU - Meister, B
AU  - Meister B
FAU - Berggren, P O
AU  - Berggren PO
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Surface)
RN  - 0 (Calcium Channels)
RN  - 0 (Calcium Channels, L-Type)
RN  - 0 (Luminescent Proteins)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Stx1a protein, mouse)
RN  - 0 (Syntaxin 1)
RN  - 0 (Tubulin)
RN  - 147336-22-9 (Green Fluorescent Proteins)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/pharmacology
MH  - Antigens, Surface/immunology/isolation & purification/*metabolism
MH  - Calcium/metabolism
MH  - Calcium Channels/genetics/isolation & purification/*physiology
MH  - Calcium Channels, L-Type
MH  - Cell Membrane/physiology/ultrastructure
MH  - Centrifugation, Density Gradient
MH  - Exocytosis/physiology
MH  - Green Fluorescent Proteins
MH  - Islets of Langerhans/*physiology
MH  - Luminescent Proteins/genetics
MH  - Macromolecular Substances
MH  - Mice
MH  - Mice, Obese
MH  - Nerve Tissue Proteins/immunology/isolation & purification/*metabolism
MH  - Patch-Clamp Techniques
MH  - Recombinant Fusion Proteins/metabolism
MH  - Syntaxin 1
MH  - Tubulin/immunology/physiology
PMC - PMC17860
EDAT- 1999/09/01 00:00
MHDA- 1999/09/01 00:01
CRDT- 1999/09/01 00:00
PHST- 1999/09/01 00:00 [pubmed]
PHST- 1999/09/01 00:01 [medline]
PHST- 1999/09/01 00:00 [entrez]
AID - 10.1073/pnas.96.18.10164 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 Aug 31;96(18):10164-9. doi:
      10.1073/pnas.96.18.10164.