Biology:GP1BA

From HandWiki
Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Platelet glycoprotein Ib alpha chain also known as glycoprotein Ib (platelet), alpha polypeptide or CD42b (Cluster of Differentiation 42b), is a protein that in humans is encoded by the GP1BA gene.

Function

Glycoprotein Ib (GP Ib) is a platelet surface membrane glycoprotein receptor composed of a heterodimer, an alpha chain and a beta chain, that are linked by disulfide bonds.[1] The Gp Ib functions as a receptor for von Willebrand factor (VWF). The complete receptor complex includes noncovalent association of the alpha and beta subunits with platelet glycoprotein IX and platelet glycoprotein V to form the glycoprotein Ib-IX-V complex. Binding of the GP Ib-IX-V complex to VWF facilitates initial platelet adhesion to vascular subendothelium after vascular injury,[2] and also initiates signaling events within the platelet that lead to enhanced platelet activation, thrombosis, and hemostasis.[3] This gene encodes the alpha subunit. Several polymorphisms and mutations have been described in this gene, some of which are the cause of Bernard–Soulier syndromes and platelet-type von Willebrand disease.[4]

Interactions

GP1BA has been shown to interact with YWHAZ[5][6][7] and FLNB.[8]

See also

References

  1. "Cloning of the alpha chain of human platelet glycoprotein Ib: a transmembrane protein with homology to leucine-rich alpha 2-glycoprotein". Proceedings of the National Academy of Sciences of the United States of America 84 (16): 5615–5619. August 1987. doi:10.1073/pnas.84.16.5615. PMID 3303030. Bibcode1987PNAS...84.5615L. 
  2. "Ultralarge multimers of von Willebrand factor form spontaneous high-strength bonds with the platelet glycoprotein Ib-IX complex: studies using optical tweezers". Blood 99 (11): 3971–3977. June 2002. doi:10.1182/blood-2001-11-0060. PMID 12010796. https://ashpublications.org/blood/article/99/11/3971/106884/Ultralarge-multimers-of-von-Willebrand-factor-form. Retrieved 2023-09-08. 
  3. "Signaling events underlying thrombus formation". Journal of Thrombosis and Haemostasis 1 (7): 1602–1612. July 2003. doi:10.1046/j.1538-7836.2003.00267.x. PMID 12871297. 
  4. "Entrez Gene: GP1BA glycoprotein Ib (platelet), alpha polypeptide". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2811. 
  5. "Human signaling protein 14-3-3zeta interacts with platelet glycoprotein Ib subunits Ibalpha and Ibbeta". Blood 91 (4): 1295–1303. February 1998. doi:10.1182/blood.V91.4.1295. PMID 9454760. 
  6. "Identification of a binding sequence for the 14-3-3 protein within the cytoplasmic domain of the adhesion receptor, platelet glycoprotein Ib alpha". The Journal of Biological Chemistry 271 (13): 7362–7367. March 1996. doi:10.1074/jbc.271.13.7362. PMID 8631758. 
  7. "Cytoplasmic domains of GpIbalpha and GpIbbeta regulate 14-3-3zeta binding to GpIb/IX/V". Blood 95 (2): 551–557. January 2000. doi:10.1182/blood.V95.2.551. PMID 10627461. 
  8. "Human beta-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein Ibalpha". The Journal of Biological Chemistry 273 (28): 17531–17538. July 1998. doi:10.1074/jbc.273.28.17531. PMID 9651345. 

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.