FERMT2

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Fermitin family homolog 2 (FERMT2) also known as pleckstrin homology domain-containing family C member 1 (PLEKHC1) or kindlin-2 is a protein that in humans is encoded by the FERMT2 gene.[1][2][3]

Kindlin-2 is the first of the kindlin protein to be discovered in 1994. It was detected in a screen for epidermal growth factor (EGF)-induced mRNAs and initially named mitogen-inducible gene 2 (Mig-2) protein.[1]

Function

FERMT2 is a component of extracellular matrix structures in mammalian cells and is required for proper control of cell shape change.[4]

A major task of kindlins is to regulate the activation of integrins.[5]

Interactions

FERMT2 has been shown to interact with FBLIM1.[4]

Role in health and diseases

  • Loss of kindlin-2 in mice leads to peri-implantation lethality.[6]
  • Kindlin-2 is highly expressed in activated myofibroblasts for regulation of focal adhesion formation.[7]
  • Deletion of Kindlin-2 retards insulin secretion and reduces β-cell mass in mice.[8]
  • Elevated kindlin-2 expression was observed in tubular intestinal fibrosis of the kidney, a condition is characterized by massive expansion of the cortical interstitium, conversion of fibroblasts into myofibroblasts and progressive EMT of tubular epithelial cells.[9]
  • Kindlin-2 is required for angiogenesis and blood vessel homeostasis.[10]
  • Kindlin-2 can exert tumor-promoting or tumor-inhibiting functions based on tumor-type-dependent.[11]
  • FERMT2 modulates the Alzheimer's Disease risk by regulating APP metabolism and Aβ peptide production.[12]


References

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  1. ^ a b Page Module:Citation/CS1/styles.css has no content.Wick M, Bürger C, Brüsselbach S, Lucibello FC, Müller R (January 1994). "Identification of serum-inducible genes: different patterns of gene regulation during G0→S and G1→S progression". Journal of Cell Science. 107 ( Pt 1) (1): 227–39. doi:10.1242/jcs.107.1.227. PMID 8175911.
  2. ^ Page Module:Citation/CS1/styles.css has no content.Weinstein EJ, Bourner M, Head R, Zakeri H, Bauer C, Mazzarella R (April 2003). "URP1: a member of a novel family of PH and FERM domain-containing membrane-associated proteins is significantly over-expressed in lung and colon carcinomas". Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1637 (3): 207–16. doi:10.1016/S0925-4439(03)00035-8. PMID 12697302.
  3. ^ Page Module:Citation/CS1/styles.css has no content."Entrez Gene: FERMT2".
  4. ^ a b Page Module:Citation/CS1/styles.css has no content.Tu Y, Wu S, Shi X, Chen K, Wu C (April 2003). "Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation". Cell. 113 (1): 37–47. doi:10.1016/S0092-8674(03)00163-6. PMID 12679033.
  5. ^ Page Module:Citation/CS1/styles.css has no content.Rognoni E, Ruppert R, Fässler R (January 2016). "The kindlin family: functions, signaling properties and implications for human disease". Journal of Cell Science. 129 (1): 17–27. doi:10.1242/jcs.161190. PMID 26729028.
  6. ^ Page Module:Citation/CS1/styles.css has no content.Montanez E, Ussar S, Schifferer M, Bösl M, Zent R, Moser M, Fässler R (May 2008). "Kindlin-2 controls bidirectional signaling of integrins". Genes & Development. 22 (10): 1325–30. doi:10.1101/gad.469408. PMC 2377186. PMID 18483218.
  7. ^ Page Module:Citation/CS1/styles.css has no content.He Y, Esser P, Schacht V, Bruckner-Tuderman L, Has C (January 2011). "Role of kindlin-2 in fibroblast functions: implications for wound healing". The Journal of Investigative Dermatology. 131 (1): 245–56. doi:10.1038/jid.2010.273. PMID 20861856.
  8. ^ Page Module:Citation/CS1/styles.css has no content.Zhu K, Lai Y, Cao H, Bai X, Liu C, Yan Q, et al. (January 2020). "Kindlin-2 modulates MafA and β-catenin expression to regulate β-cell function and mass in mice". Nature Communications. 11 (1): 484. Bibcode:2020NatCo..11..484Z. doi:10.1038/s41467-019-14186-y. PMC 6981167. PMID 31980627.
  9. ^ Page Module:Citation/CS1/styles.css has no content.Bielesz B, Sirin Y, Si H, Niranjan T, Gruenwald A, Ahn S, Kato H, Pullman J, Gessler M, Haase VH, Susztak K (November 2010). "Epithelial Notch signaling regulates interstitial fibrosis development in the kidneys of mice and humans". The Journal of Clinical Investigation. 120 (11): 4040–54. doi:10.1172/JCI43025. PMC 2964979. PMID 20978353.
  10. ^ Page Module:Citation/CS1/styles.css has no content.Pluskota E, Dowling JJ, Gordon N, Golden JA, Szpak D, West XZ, Nestor C, Ma YQ, Bialkowska K, Byzova T, Plow EF (May 2011). "The integrin coactivator kindlin-2 plays a critical role in angiogenesis in mice and zebrafish". Blood. 117 (18): 4978–87. doi:10.1182/blood-2010-11-321182. PMC 3100704. PMID 21378273.
  11. ^ Page Module:Citation/CS1/styles.css has no content.Zhan J, Zhang H (May 2018). "Kindlins: Roles in development and cancer progression". The International Journal of Biochemistry & Cell Biology. 98: 93–103. doi:10.1016/j.biocel.2018.03.008. PMID 29544897.
  12. ^ DOI = 10.1007/s00401-016-1652-z

Further reading

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