Biology:Erbin (protein)

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Short description: Protein found in humans


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

Erbb2 interacting protein (ERBB2IP), also known as erbin, is a protein which in humans is encoded by the ERBB2IP gene.[1] Discovered in 1997, erbin is a 200kDa protein containing a PDZ domain.[2]

Function

This gene is a member of the leucine-rich repeat and PDZ domain (LAP) family. The encoded protein contains 17 leucine-rich repeats and one PDZ domain. It binds to the unphosphorylated form of the ERBB2 protein and regulates ERBB2 function and localization. It has also been shown to affect the Ras signaling pathway by disrupting Ras-Raf interaction. Alternate transcriptional splice variants encoding different isoforms have been found for this gene, but only two of them have been characterized to date.[1]

Clinical significance

Erbin's C-terminal PDZ domain is able to bind to ErbB2, a protein tyrosine kinase which is often associated with poor prognosis in epidermal oncogenesis.[3] Erbin's N-terminal region has been shown to disrupt Ras to Raf binding and may be, through this action, a tumor suppressing protein.[4]

Interactions

Erbin has been shown to interact with:

References

  1. 1.0 1.1 "Entrez Gene: ERBB2IP erbb2 interacting protein". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55914. 
  2. "ERBIN: a basolateral PDZ protein that interacts with the mammalian ERBB2/HER2 receptor". Nat. Cell Biol. 2 (7): 407–414. 2000. doi:10.1038/35017038. PMID 10878805. https://hal.inrae.fr/hal-02695847/file/2000_Borg_NatureCellBiol_1.pdf. 
  3. "Erbin: sorting out ErbB2 receptors or giving Ras a break?". Sci STKE 2003 (199): pe37. 2003. doi:10.1126/stke.2003.199.pe37. PMID 12966186. 
  4. "Erbin inhibits RAF activation by disrupting the sur-8-Ras-Raf complex". J. Biol. Chem. 281 (2): 927–933. 2006. doi:10.1074/jbc.M507360200. PMID 16301319. 
  5. 5.0 5.1 "The hemidesmosomal protein bullous pemphigoid antigen 1 and the integrin beta 4 subunit bind to ERBIN. Molecular cloning of multiple alternative splice variants of ERBIN and analysis of their tissue expression". J. Biol. Chem. 276 (35): 32427–36. August 2001. doi:10.1074/jbc.M011005200. PMID 11375975. 
  6. "The ERBB2/HER2 receptor differentially interacts with ERBIN and PICK1 PSD-95/DLG/ZO-1 domain proteins". J. Biol. Chem. 276 (18): 15256–63. May 2001. doi:10.1074/jbc.M010032200. PMID 11278603. http://prodinra.inra.fr/ft/1478A66C-AC9E-4818-B9CC-97753E19BBE6. 
  7. "ERBIN: a basolateral PDZ protein that interacts with the mammalian ERBB2/HER2 receptor". Nat. Cell Biol. 2 (7): 407–14. July 2000. doi:10.1038/35017038. PMID 10878805. https://hal.inrae.fr/hal-02695847/file/2000_Borg_NatureCellBiol_1.pdf. 
  8. "Erbin suppresses the MAP kinase pathway". J. Biol. Chem. 278 (2): 1108–14. January 2003. doi:10.1074/jbc.M205413200. PMID 12379659. 
  9. "Identification of three novel Smad binding proteins involved in cell polarity". FEBS Lett. 539 (1–3): 167–73. March 2003. doi:10.1016/s0014-5793(03)00155-8. PMID 12650946. 
  10. "ERBIN associates with p0071, an armadillo protein, at cell-cell junctions of epithelial cells". Genes Cells 7 (5): 475–85. May 2002. doi:10.1046/j.1365-2443.2002.00533.x. PMID 12047349. 
  11. "Interaction between Erbin and a Catenin-related protein in epithelial cells". J. Biol. Chem. 277 (4): 2869–75. January 2002. doi:10.1074/jbc.M109652200. PMID 11711544. 
  12. "The Erbin PDZ domain binds with high affinity and specificity to the carboxyl termini of delta-catenin and ARVCF". J. Biol. Chem. 277 (15): 12906–14. April 2002. doi:10.1074/jbc.M200818200. PMID 11821434. 
  13. Stevens, Payton D.; Wen, Yang-An; Xiong, Xiaopeng; Zaytseva, Yekaterina Y.; Li, Austin T.; Wang, Chi; Stevens, Ashley T.; Farmer, Trevor N. et al. (September 1, 2018). "Erbin Suppresses KSR1-Mediated RAS/RAF Signaling and Tumorigenesis in Colorectal Cancer". Cancer Research 78 (17): 4839–4852. doi:10.1158/0008-5472.CAN-17-3629. ISSN 1538-7445. PMID 29980571. 

Further reading

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