PMID- 10627461
OWN - NLM
STAT- MEDLINE
DCOM- 20000203
LR  - 20131121
IS  - 0006-4971 (Print)
IS  - 0006-4971 (Linking)
VI  - 95
IP  - 2
DP  - 2000 Jan 15
TI  - Cytoplasmic domains of GpIbalpha and GpIbbeta regulate 14-3-3zeta binding to
      GpIb/IX/V.
PG  - 551-7
AB  - Shear stress causes the platelet glycoprotein (Gp) Ib/IX/V to bind to von
      Willebrand factor, resulting in platelet adhesion. GpIb/IX/V also functions to
      stimulate transmembranous signaling, leading to platelet activation and the
      expression of a ligand-receptive GpIIb-IIIa complex. The highly conserved
      cytoplasmic domain of GpIbalpha binds directly to a dimeric 14-3-3 adapter
      protein zeta isoform. To explore structural determinants of GpIb/IX/V binding to 
      14-3-3zeta, the authors examined 14-3-3zeta interactions with GpIbalpha and
      GpIbbeta in heterologous cells and platelets. Truncations of GpIbalpha at amino
      acid 542 or 594, or deletions of residues 542 through 590, inhibited binding of
      14-3-3zeta. Deletion of GpIbalpha from Trp(570) to Ser(590) eliminated 14-3-3zeta
      binding, and deletion of the sequence from Arg(542)-Trp(570) enhanced binding of 
      14-3-3zeta to GpIbalpha. All GpIbalpha mutations that eliminated GpIbalpha
      binding to the GST-14-3-3zeta fusion protein also eliminated GpIbbeta binding to 
      the fusion protein. Forskolin treatment of Chinese hamster ovary cells expressing
      wild-type GpIbalpha/beta/IX resulted in the phosphorylation of GpIbbeta
      associated with enhanced binding of GpIbbeta to GST-14-3-3zeta fusion protein and
      increased 14-3-3zeta coimmunoprecipitated with GpIbalpha. When intact human
      platelets aggregated in response to 90 dynes/cm(2) shear stress, 14-3-3zeta
      disassociated from GpIbalpha. Prostacyclin treatment of platelets inhibited shear
      stress-induced aggregation and the release of 14-3-3zeta from GpIbalpha. These
      data demonstrate that amino acid residues in the cytoskeletal interaction domains
      of GpIbalpha regulate 14-3-3zeta binding to GpIbalpha/beta/IX, and suggest that
      protein kinase A-dependent phosphorylation of GpIbbeta enhances 14-3-3zeta
      binding to the GpIb/IX/V complex in human platelets. (Blood. 2000;95:551-557)
FAU - Feng, S
AU  - Feng S
AD  - Veterans Administration Medical Center, Baylor College of Medicine and Rice
      University, Houston, TX 77030, USA.
FAU - Christodoulides, N
AU  - Christodoulides N
FAU - Resendiz, J C
AU  - Resendiz JC
FAU - Berndt, M C
AU  - Berndt MC
FAU - Kroll, M H
AU  - Kroll MH
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Blood
JT  - Blood
JID - 7603509
RN  - 0 (14-3-3 Proteins)
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Platelet Glycoprotein GPIb-IX Complex)
RN  - 0 (Proteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 1F7A44V6OU (Colforsin)
RN  - EC 1.14.16.2 (Tyrosine 3-Monooxygenase)
SB  - AIM
SB  - IM
SB  - S
MH  - 14-3-3 Proteins
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Blood Platelets/physiology
MH  - CHO Cells
MH  - Colforsin/pharmacology
MH  - Cricetinae
MH  - Dimerization
MH  - Dogs
MH  - Enzyme Inhibitors/chemistry/*metabolism
MH  - Humans
MH  - Mice
MH  - Molecular Sequence Data
MH  - Platelet Glycoprotein GPIb-IX Complex/*chemistry/genetics/*metabolism
MH  - Polymerase Chain Reaction
MH  - Proteins/*chemistry/*metabolism
MH  - Recombinant Fusion Proteins/chemistry/metabolism
MH  - Sequence Alignment
MH  - Sequence Deletion
MH  - Sequence Homology, Amino Acid
MH  - Stress, Mechanical
MH  - Transfection
MH  - *Tyrosine 3-Monooxygenase
EDAT- 2000/01/11 00:00
MHDA- 2000/01/11 00:01
CRDT- 2000/01/11 00:00
PHST- 2000/01/11 00:00 [pubmed]
PHST- 2000/01/11 00:01 [medline]
PHST- 2000/01/11 00:00 [entrez]
PST - ppublish
SO  - Blood. 2000 Jan 15;95(2):551-7.