FERMT2

Last updated
FERMT2
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases FERMT2 , KIND2, MIG2, PLEKHC1, UNC112, UNC112B, mig-2, fermitin family member 2, URP2SF
External IDs OMIM: 607746 MGI: 2385001 HomoloGene: 4976 GeneCards: FERMT2
Gene location (Human)
Ideogram human chromosome 14.svg
Chr. Chromosome 14 (human) [1]
Human chromosome 14 ideogram.svg
HSR 1996 II 3.5e.svg
Red rectangle 2x18.png
Band 14q22.1Start52,857,268 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 Mb Chr 14: 45.46 – 45.53 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/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]

Contents

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

Related Research Articles

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FARP2 protein-coding gene in the species Homo sapiens

FERM, RhoGEF and pleckstrin domain-containing protein 2 is a protein that in humans is encoded by the FARP2 gene.

FERMT3 protein-coding gene in the species Homo sapiens

Fermitin family homolog 3) (FERMT3), also known as kindlin-3 (KIND3), MIG2-like protein (MIG2B), or unc-112-related protein 2 (URP2) is a protein that in humans is encoded by the FERMT3 gene. The kindlin family of proteins, member of the B4.1 superfamily, comprises three conserved protein homologues, kindlin 1, 2, and 3. They each contain a bipartite FERM domain comprising four subdomains F0, F1, F2, and F3 that show homology with the FERM head (H) domain of the cytoskeletal Talin protein. Kindlins have been linked to Kindler syndrome, leukocyte adhesion deficiency, cancer and other acquired human diseases. They are essential in the organisation of focal adhesions that mediate cell-extracellular matrix junctions and are involved in other cellular compartments that control cell-cell contacts and nucleus functioning. Therefore, they are responsible for cell to cell crosstalk via cell-cell contacts and integrin mediated cell adhesion through focal adhesion proteins and as specialised adhesion structures of hematopoietic cells they are also present in podosome's F actin surrounding ring structure. Isoform 2 may act as a repressor of NF-kappa-B and apoptosis

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000073712 - Ensembl, May 2017
  2. 1 2 3 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. 1 2 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. 1 2 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 . 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