FERMT2

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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)
Chromosome 14 (human)
Chr.Chromosome 14 (human)[1]
Chromosome 14 (human)
Genomic location for FERMT2
Genomic location for FERMT2
Band14q22.1Start52,857,268 bp[1]
End52,952,435 bp[1]
RNA expression pattern
PBB GE PLEKHC1 214212 x at fs.png

PBB GE PLEKHC1 209210 s at fs.png

PBB GE PLEKHC1 209209 s at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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

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]

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[edit]

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[edit]

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

Role in health and diseases[edit]

  • 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]
  • 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.[12]
  • Kindlin-2 is required for angiogenesis and blood vessel homeostasis.[13]
  • Kindlin-2 can exert tumor-promoting or tumor-inhibiting functions based on tumor-type-dependent.[14]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000073712 - Ensembl, May 2017
  2. ^ a b c 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. ^ a b 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. 1637 (3): 207–16. doi:10.1016/S0925-4439(03)00035-8. PMID 12697302.
  7. ^ "Entrez Gene: FERMT2".
  8. ^ a b 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. ^ 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.
  13. ^ 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.
  14. ^ 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[edit]

  • 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>

External links[edit]