FERMT2

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.[5][6][7]

FERMT2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesFERMT2, KIND2, MIG2, PLEKHC1, UNC112, UNC112B, mig-2, fermitin family member 2, URP2SF
External IDsOMIM: 607746 MGI: 2385001 HomoloGene: 4976 GeneCards: FERMT2
Gene location (Human)
Chr.Chromosome 14 (human)[1]
Band14q22.1Start52,857,268 bp[1]
End52,952,435 bp[1]
RNA expression pattern




More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

10979

218952

Ensembl

ENSG00000073712

ENSMUSG00000037712

UniProt

Q96AC1

Q8CIB5

RefSeq (mRNA)

NM_001134999
NM_001135000
NM_006832

NM_146054
NM_001360525
NM_001360526

RefSeq (protein)

NP_001128471
NP_001128472
NP_006823

NP_666166
NP_001347454
NP_001347455

Location (UCSC)Chr 14: 52.86 – 52.95 MbChr 14: 45.46 – 45.53 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[5]

Function

FERMT2 is a component of extracellular matrix structures in mammalian cells and is required for proper control of cell shape change.[8]

A major task of kindlins is to regulate the activation of integrins.[9]

Interactions

FERMT2 has been shown to interact with FBLIM1.[8]

Role in health and diseases
  • Loss of kindlin-2 in mice leads to peri-implantation lethality.[10]
  • Kindlin-2 is highly expressed in activated myofibroblasts for regulation of focal adhesion formation.[11]
  • Deletion of Kindlin-2 retards insulin secretion and reduces β-cell mass in mice.[12]
  • 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.[13]
  • Kindlin-2 is required for angiogenesis and blood vessel homeostasis.[14]
  • Kindlin-2 can exert tumor-promoting or tumor-inhibiting functions based on tumor-type-dependent.[15]

References
  1. GRCh38: Ensembl release 89: ENSG00000073712 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000037712 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 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. PMID 8175911.
  6. 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.
  7. "Entrez Gene: FERMT2".
  8. 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.
  9. 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.
  10. 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.
  11. 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.
  12. 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. doi:10.1038/s41467-019-14186-y. PMC 6981167. PMID 31980627.
  13. 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.
  14. 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.
  15. 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.

Further reading
  • Kato K, Shiozawa T, Mitsushita J, Toda A, Horiuchi A, Nikaido T, Fujii S, Konishi I (January 2004). "Expression of the mitogen-inducible gene-2 (mig-2) is elevated in human uterine leiomyomas but not in leiomyosarcomas". Human Pathology. 35 (1): 55–60. doi:10.1016/j.humpath.2003.08.019. PMID 14745725.
  • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (November 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
  • Wang L, Deng W, Shi T, Ma D (April 2008). "URP2SF, a FERM and PH domain containing protein, regulates NF-kappaB and apoptosis". Biochemical and Biophysical Research Communications. 368 (4): 899–906. doi:10.1016/j.bbrc.2008.02.024. PMID 18280249.</ref>
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.