PMID- 10611319
OWN - NLM
STAT- MEDLINE
DCOM- 20000127
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 26
DP  - 1999 Dec 21
TI  - Modulation of Ca(2+) entry by polypeptides of the inositol 1,4, 5-trisphosphate
      receptor (IP3R) that bind transient receptor potential (TRP): evidence for roles 
      of TRP and IP3R in store depletion-activated Ca(2+) entry.
PG  - 14955-60
AB  - Homologues of Drosophilia transient receptor potential (TRP) have been proposed
      to be unitary subunits of plasma membrane ion channels that are activated as a
      consequence of active or passive depletion of Ca(2+) stores. In agreement with
      this hypothesis, cells expressing TRPs display novel Ca(2+)-permeable cation
      channels that can be activated by the inositol 1,4,5-trisphosphate receptor
      (IP3R) protein. Expression of TRPs alters cells in many ways, including
      up-regulation of IP3Rs not coded for by TRP genes, and proof that TRP forms
      channels of these and other cells is still missing. Here, we document physical
      interaction of TRP and IP3R by coimmunoprecipitation and glutathione
      S-transferase-pulldown experiments and identify two regions of IP3R, F2q and F2g,
      that interact with one region of TRP, C7. These interacting regions were
      expressed in cells with an unmodified complement of TRPs and IP3Rs to study their
      effect on agonist- as well as store depletion-induced Ca(2+) entry and to test
      for a role of their respective binding partners in Ca(2+) entry. C7 and an
      F2q-containing fragment of IP3R decreased both forms of Ca(2+) entry. In
      contrast, F2g enhanced the two forms of Ca(2+) entry. We conclude that store
      depletion-activated Ca(2+) entry occurs through channels that have TRPs as one of
      their normal structural components, and that these channels are directly
      activated by IP3Rs. IP3Rs, therefore, have the dual role of releasing Ca(2+) from
      stores and activating Ca(2+) influx in response to either increasing IP3 or
      decreasing luminal Ca(2+).
FAU - Boulay, G
AU  - Boulay G
AD  - Department of Anesthesiology, University of California, Los Angeles, CA 90095,
      USA.
FAU - Brown, D M
AU  - Brown DM
FAU - Qin, N
AU  - Qin N
FAU - Jiang, M
AU  - Jiang M
FAU - Dietrich, A
AU  - Dietrich A
FAU - Zhu, M X
AU  - Zhu MX
FAU - Chen, Z
AU  - Chen Z
FAU - Birnbaumer, M
AU  - Birnbaumer M
FAU - Mikoshiba, K
AU  - Mikoshiba K
FAU - Birnbaumer, L
AU  - Birnbaumer L
LA  - eng
GR  - DK41244/DK/NIDDK NIH HHS/United States
GR  - GM54235/GM/NIGMS NIH HHS/United States
GR  - HL45195/HL/NHLBI NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
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 (Calcium Channels)
RN  - 0 (Inositol 1,4,5-Trisphosphate Receptors)
RN  - 0 (Receptors, Cytoplasmic and Nuclear)
RN  - 0 (TRPC Cation Channels)
RN  - 0 (transient receptor potential cation channel, subfamily C, member 1)
RN  - SY7Q814VUP (Calcium)
SB  - IM
CIN - Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14669-71. PMID: 10611268
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Biological Transport
MH  - Calcium/*metabolism
MH  - Calcium Channels/*metabolism
MH  - Cell Polarity
MH  - Inositol 1,4,5-Trisphosphate Receptors
MH  - Models, Biological
MH  - Molecular Sequence Data
MH  - Precipitin Tests
MH  - Protein Binding
MH  - Receptors, Cytoplasmic and Nuclear/*metabolism
MH  - Sequence Homology, Amino Acid
MH  - TRPC Cation Channels
PMC - PMC24754
EDAT- 1999/12/28 00:00
MHDA- 1999/12/28 00:01
CRDT- 1999/12/28 00:00
PHST- 1999/12/28 00:00 [pubmed]
PHST- 1999/12/28 00:01 [medline]
PHST- 1999/12/28 00:00 [entrez]
AID - 10.1073/pnas.96.26.14955 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14955-60. doi:
      10.1073/pnas.96.26.14955.