FERMT2

FERMT2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2LGX, 2LKO, 2MSU, 4F7H
Identifiers
Aliases	FERMT2, KIND2, MIG2, PLEKHC1, UNC112, UNC112B, mig-2, fermitin family member 2, URP2SF, FERM domain containing kindlin 2
External IDs	OMIM: 607746 MGI: 2385001 HomoloGene: 4976 GeneCards: FERMT2
Gene location (Human)
Chr.	Chromosome 14 (human)[1]
End	52,952,435 bp[1]
Gene location (Mouse)
Chr.	Chromosome 14 (mouse)[2]
End	45,767,575 bp[2]
RNA expression pattern
	Top expressed in
	metanephric glomerulus; ; saphenous vein; ; parietal pleura; ; seminal vesicula; ; visceral pleura; ; tibia; ; secondary oocyte; ; vena cava; ; smooth muscle tissue; ; popliteal artery;
	Top expressed in
	left lung; ; left lung lobe; ; ankle; ; right lung lobe; ; vastus lateralis muscle; ; triceps brachii muscle; ; sternocleidomastoid muscle; ; temporal muscle; ; digastric muscle; ; atrium;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	protein binding; phosphatidylinositol-3,4,5-trisphosphate binding; lipid binding; actin filament binding;
Cellular component	cytoplasm; filamentous actin; cytosol; cell projection; membrane; I band; focal adhesion; extrinsic component of cytoplasmic side of plasma membrane; plasma membrane; stress fiber; nucleoplasm; cell surface; cell junction; cell cortex; cytoskeleton; lamellipodium membrane; nucleus;
Biological process	protein localization to membrane; Wnt signaling pathway; focal adhesion assembly; cell adhesion; regulation of cell shape; integrin-mediated signaling pathway; substrate adhesion-dependent cell spreading; integrin activation; cell-matrix adhesion; transforming growth factor beta receptor signaling pathway; cell junction assembly;
	Sources:Amigo / QuickGO
Orthologs
	10979
	218952
	ENSG00000073712
	ENSMUSG00000037712
	Q96AC1
	Q8CIB5
	NM_001134999; NM_001135000; NM_006832
	NM_146054; NM_001360525; NM_001360526
	NP_001128471; NP_001128472; NP_006823
	NP_666166; NP_001347454; NP_001347455
	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]

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]
FERMT2 modulates the Alzheimer's Disease risk by regulating APP metabolism and Aβ peptide production.[16]

References

GRCh38: Ensembl release 89: ENSG00000073712 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000037712 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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.
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.
"Entrez Gene: FERMT2".
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.
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.
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.
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.
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.
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.
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.
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.
DOI = 10.1007/s00401-016-1652-z

External links

FERMT2 Info with links in the Cell Migration Gateway Archived 2014-12-11 at the Wayback Machine

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000073712 - Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid8175911-5] 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. doi:10.1242/jcs.107.1.227. PMID 8175911.

[pmid12697302-6] 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.

[entrez-7] "Entrez Gene: FERMT2".

[pmid12679033-8] 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.

[pmid26729028-9] 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. Bibcode:2020NatCo..11..484Z. 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.

[16] DOI = 10.1007/s00401-016-1652-z