TLN1

Last updated
TLN1
Protein TLN1 PDB 1mix.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases TLN1 , ILWEQ, TLN, talin 1, talin-1
External IDs OMIM: 186745 MGI: 1099832 HomoloGene: 21267 GeneCards: TLN1
Orthologs
SpeciesHumanMouse
Entrez

7094

21894

Ensembl

ENSG00000137076

ENSMUSG00000028465

UniProt

Q9Y490

P26039

RefSeq (mRNA)

NM_006289

NM_011602

RefSeq (protein)

NP_006280

NP_035732

Location (UCSC) Chr 9: 35.7 – 35.73 Mb Chr 4: 43.53 – 43.56 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Talin-1 is a protein that in humans is encoded by the TLN1 gene. [5] [6] Talin-1 is ubiquitously expressed, and is localized to costamere structures in cardiac and skeletal muscle cells, and to focal adhesions in smooth muscle and non-muscle cells. Talin-1 functions to mediate cell-cell adhesion via the linkage of integrins to the actin cytoskeleton and in the activation of integrins. Altered expression of talin-1 has been observed in patients with heart failure, however no mutations in TLN1 have been linked with specific diseases.

Contents

Structure

Human talin-1 is 270.0 kDa molecular weight and 2541 amino acids. [7] The N-terminal region of talin-1 is ~50 kDa in size and homologous to members of the ERM protein family which have a globular FERM domain (residues 86-400) that links the actin cytoskeleton to adhesion proteins. [8] [9] In addition to F-actin, [10] the N-terminal region of talin-1 binds layilin, [11] β1- and β3-integrin, [12] [13] [14] and focal adhesion kinase. [15] [16] Talin-1 N-terminal region also binds acidic phospholipids for insertion into lipid bilayers. [17] [18] [19] The rod domain (>200 kDa) has considerable flexibility and houses a conserved actin binding site, [10] three vinculin binding sites, [20] [21] [22] and also has an additional integrin binding site, termed IBS2. [23] [24] [25] [26] [27] The head and rod domains are connected by an unstructured linker region (residues 401-481), which houses several sites of phosphorylation, [28] as well as protease cleavage. [29] Talin-1 can homodimerize in an antiparallel fashion, [30] however, talin-1 and its closely related counterpart, talin-2 do not form heterodimers. [31]

Function

In mammals talin-1 is ubiquitously expressed; talin-1 is found complexed to integrins and localized to intercalated discs of cardiac muscle and to costamere structures of both skeletal and cardiac muscles, [32] in correspondence with the I-band and M-line. [33] [34] [35] Talin-1 is also found at focal adhesions of smooth muscle cells [36] and non-muscle cells. [9]

In undifferentiated cultures of myoblasts, talin-1 expression is perinuclear, and then progresses to a cytoplasmic distribution followed by a sarcomlemmal, costameric-like pattern by day 15 of differentiation. [37] Homozygous disruption of TLN1 in mice is embryonic lethal, demonstrating that talin-1 is required for normal embryogenesis. [38] It has been shown, however, that talin-1 expression is minor in adult cardiomyocytes, and becomes more prominent at costameres during cardiac hypertrophy induced by pharmacological and mechanical stress. [39]

The primary function of talin-1 involves the linkage of integrins to the actin cytoskeleton and in the energy-dependent activation of integrins. [9] [40] Functions for talin-1 in specific tissues have been illuminated through conditional knockout animals. Studies employing the conditional knockout of talin 1 in skeletal muscle have demonstrated its role in maintaining integrin attachment sites at myotendinous junctions; knockout mice develop progressive myopathy and show deficits in muscle force generation. [41] In platelets, conditional knockout of talin-1 results in the inability to activate integrins in response to platelet agonists, resulting in mice with severe hemostatic defects and resistance to arterial thrombosis. [42] Conditional knockout of talin-1 in cardiomyocytes shows that mice have normal cardiac function at baseline, but improved function, blunted hypertrophy, and attenuated fibrosis when subjected to pressure overload-induced cardiac hypertrophy, which correlated with blunted ERK1/2, p38, Akt, and glycogen synthase kinase 3 responses. These data suggest that upregulation of talin-1 in cardiac hypertrophy may be detrimental to cardiomyocytes function. [39]

Clinical significance

In patients with heart failure, talin-1 expression in cardiomyocytes is increased relative to control cells. [39]

Interactions

TLN1 has been shown to interact with:

See also

Related Research Articles

<span class="mw-page-title-main">Integrin</span> Instance of a defined set in Homo sapiens with Reactome ID (R-HSA-374573)

Integrins are transmembrane receptors that help cell-cell and cell-extracellular matrix (ECM) adhesion. Upon ligand binding, integrins activate signal transduction pathways that mediate cellular signals such as regulation of the cell cycle, organization of the intracellular cytoskeleton, and movement of new receptors to the cell membrane. The presence of integrins allows rapid and flexible responses to events at the cell surface.

<span class="mw-page-title-main">Vinculin</span> Mammalian protein found in Homo sapiens

In mammalian cells, vinculin is a membrane-cytoskeletal protein in focal adhesion plaques that is involved in linkage of integrin adhesion molecules to the actin cytoskeleton. Vinculin is a cytoskeletal protein associated with cell-cell and cell-matrix junctions, where it is thought to function as one of several interacting proteins involved in anchoring F-actin to the membrane.

<span class="mw-page-title-main">Focal adhesion</span>

In cell biology, focal adhesions are large macromolecular assemblies through which mechanical force and regulatory signals are transmitted between the extracellular matrix (ECM) and an interacting cell. More precisely, focal adhesions are the sub-cellular structures that mediate the regulatory effects of a cell in response to ECM adhesion.

<span class="mw-page-title-main">Paxillin</span> Protein-coding gene in the species Homo sapiens

Paxillin is a protein that in humans is encoded by the PXN gene. Paxillin is expressed at focal adhesions of non-striated cells and at costameres of striated muscle cells, and it functions to adhere cells to the extracellular matrix. Mutations in PXN as well as abnormal expression of paxillin protein has been implicated in the progression of various cancers.

Actinin is a microfilament protein. The functional protein is an anti-parallel dimer, which cross-links the thin filaments in adjacent sarcomeres, and therefore coordinates contractions between sarcomeres in the horizontal axis. Alpha-actinin is a part of the spectrin superfamily. This superfamily is made of spectrin, dystrophin, and their homologous and isoforms. In non-muscle cells, it is found by the actin filaments and at the adhesion sites.The lattice like arrangement provides stability to the muscle contractile apparatus. Specifically, it helps bind actin filaments to the cell membrane. There is a binding site at each end of the rod and with bundles of actin filaments.

<span class="mw-page-title-main">Costamere</span> Component of striated muscle cells

The costamere is a structural-functional component of striated muscle cells which connects the sarcomere of the muscle to the cell membrane.

<span class="mw-page-title-main">Integrin-linked kinase</span> Protein-coding gene in the species Homo sapiens

Integrin-linked kinase is an enzyme that in humans is encoded by the ILK gene involved with integrin-mediated signal transduction. Mutations in ILK are associated with cardiomyopathies. It is a 59kDa protein originally identified in a yeast-two hybrid screen with integrin β1 as the bait protein. Since its discovery, ILK has been associated with multiple cellular functions including cell migration, proliferation, and adhesion.

<span class="mw-page-title-main">Integrin beta 1</span> Mammalian protein found in Homo sapiens

Integrin beta-1 (ITGB1), also known as CD29, is a cell surface receptor that in humans is encoded by the ITGB1 gene. This integrin associates with integrin alpha 1 and integrin alpha 2 to form integrin complexes which function as collagen receptors. It also forms dimers with integrin alpha 3 to form integrin receptors for netrin 1 and reelin. These and other integrin beta 1 complexes have been historically known as very late activation (VLA) antigens.

Talin is a high-molecular-weight cytoskeletal protein concentrated at regions of cell–substratum contact and, in lymphocytes, at cell–cell contacts. Discovered in 1983 by Keith Burridge and colleagues, talin is a ubiquitous cytosolic protein that is found in high concentrations in focal adhesions. It is capable of linking integrins to the actin cytoskeleton either directly or indirectly by interacting with vinculin and α-actinin.

<span class="mw-page-title-main">PTK2</span> Protein-coding gene in humans

PTK2 protein tyrosine kinase 2 (PTK2), also known as focal adhesion kinase (FAK), is a protein that, in humans, is encoded by the PTK2 gene. PTK2 is a focal adhesion-associated protein kinase involved in cellular adhesion and spreading processes. It has been shown that when FAK was blocked, breast cancer cells became less metastatic due to decreased mobility.

<span class="mw-page-title-main">TGFB1I1</span> Protein-coding gene in the species Homo sapiens

Transforming growth factor beta-1-induced transcript 1 protein is a protein that in humans is encoded by the TGFB1I1 gene. Often put together with and studied alongside TGFB1I1 is the mouse homologue HIC-5. As the name suggests, TGFB1I1 is an induced form of the larger family of TGFB1. Studies suggest TGFB1I1 plays a role in processes of cell growth, proliferation, migration, differentiation and senescence. TGFB1I1 is most localized at focal adhesion complexes of cells, although it may be found active in the cytosol, nucleus and cell membrane as well.

<span class="mw-page-title-main">Actin, cytoplasmic 2</span> Protein-coding gene in the species Homo sapiens

Actin, cytoplasmic 2, or gamma-actin is a protein that in humans is encoded by the ACTG1 gene. Gamma-actin is widely expressed in cellular cytoskeletons of many tissues; in adult striated muscle cells, gamma-actin is localized to Z-discs and costamere structures, which are responsible for force transduction and transmission in muscle cells. Mutations in ACTG1 have been associated with nonsyndromic hearing loss and Baraitser-Winter syndrome, as well as susceptibility of adolescent patients to vincristine toxicity.

<span class="mw-page-title-main">Alpha-actinin-1</span> Protein-coding gene in the species Homo sapiens

Alpha-actinin-1 is a protein that in humans is encoded by the ACTN1 gene.

<span class="mw-page-title-main">Alpha-actinin-3</span> Mammalian protein found in Homo sapiens

Alpha-actinin-3, also known as alpha-actinin skeletal muscle isoform 3 or F-actin cross-linking protein, is a protein that in humans is encoded by the ACTN3 gene located on chromosome 11. All people have two copies (alleles) of this gene.

<span class="mw-page-title-main">Alpha-actinin-2</span> Protein-coding gene in the species Homo sapiens

Alpha-actinin-2 is a protein which in humans is encoded by the ACTN2 gene. This gene encodes an alpha-actinin isoform that is expressed in both skeletal and cardiac muscles and functions to anchor myofibrillar actin thin filaments and titin to Z-discs.

<span class="mw-page-title-main">Alpha-actinin-4</span> Protein-coding gene in the species Homo sapiens

Alpha-actinin-4 is a protein that in humans is encoded by the ACTN4 gene.

<span class="mw-page-title-main">FLNC (gene)</span> Protein-coding gene in the species Homo sapiens

Filamin-C (FLN-C) also known as actin-binding-like protein (ABPL) or filamin-2 (FLN2) is a protein that in humans is encoded by the FLNC gene. Filamin-C is mainly expressed in cardiac and skeletal muscles, and functions at Z-discs and in subsarcolemmal regions.

<span class="mw-page-title-main">Integrin alpha 7</span>

Alpha-7 integrin is a protein that in humans is encoded by the ITGA7 gene. Alpha-7 integrin is critical for modulating cell-matrix interactions. Alpha-7 integrin is highly expressed in cardiac muscle, skeletal muscle and smooth muscle cells, and localizes to Z-disc and costamere structures. Mutations in ITGA7 have been associated with congenital myopathies and noncompaction cardiomyopathy, and altered expression levels of alpha-7 integrin have been identified in various forms of muscular dystrophy.

<span class="mw-page-title-main">Catenin alpha-1</span> Protein-coding gene in the species Homo sapiens

αE-catenin, also known as Catenin alpha-1 is a protein that in humans is encoded by the CTNNA1 gene. αE-catenin is highly expressed in cardiac muscle and localizes to adherens junctions at intercalated disc structures where it functions to mediate the anchorage of actin filaments to the sarcolemma. αE-catenin also plays a role in tumor metastasis and skin cell function.

<span class="mw-page-title-main">TLN2</span> Protein-coding gene in the species Homo sapiens

Talin 2 is a protein in humans that is encoded by the TLN2 gene. It belongs to the talin protein family. This gene encodes a protein related to talin 1, a cytoskeletal protein that plays a significant role in the assembly of actin filaments. Talin-2 is expressed at high levels in cardiac muscle and functions to provide linkages between the extracellular matrix and actin cytoskeleton at costamere structures to transduce force laterally.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000137076 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028465 - 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. ↑ Gilmore AP, Ohanian V, Spurr NK, Critchley DR (Aug 1995). "Localisation of the human gene encoding the cytoskeletal protein talin to chromosome 9p". Human Genetics. 96 (2): 221–4. doi:10.1007/BF00207384. PMID   7635475. S2CID   38856479.
  6. ↑ Ben-Yosef T, Francomano CA (Dec 1999). "Characterization of the human talin (TLN) gene: genomic structure, chromosomal localization, and expression pattern". Genomics. 62 (2): 316–9. doi:10.1006/geno.1999.6019. PMID   10610730.
  7. ↑ "Protein sequence of human TLN1 (Uniprot ID: Q9Y490)". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Archived from the original on 8 July 2015. Retrieved 7 July 2015.
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  19. ↑ Heise H, Bayerl T, Isenberg G, Sackmann E (Jan 1991). "Human platelet P-235, a talin-like actin binding protein, binds selectively to mixed lipid bilayers". Biochimica et Biophysica Acta (BBA) - Biomembranes. 1061 (2): 121–31. doi:10.1016/0005-2736(91)90276-e. PMID   1900196.
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  25. ↑ Rodius S, Chaloin O, Moes M, Schaffner-Reckinger E, Landrieu I, Lippens G, Lin M, Zhang J, Kieffer N (Aug 2008). "The talin rod IBS2 alpha-helix interacts with the beta3 integrin cytoplasmic tail membrane-proximal helix by establishing charge complementary salt bridges". The Journal of Biological Chemistry. 283 (35): 24212–23. doi: 10.1074/jbc.M709704200 . PMC   3259754 . PMID   18577523.
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  38. ↑ Monkley SJ, Zhou XH, Kinston SJ, Giblett SM, Hemmings L, Priddle H, Brown JE, Pritchard CA, Critchley DR, Fässler R (Dec 2000). "Disruption of the talin gene arrests mouse development at the gastrulation stage". Developmental Dynamics. 219 (4): 560–74. doi: 10.1002/1097-0177(2000)9999:9999<::AID-DVDY1079>3.0.CO;2-Y . PMID   11084655.
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  43. ↑ Wegener KL, Basran J, Bagshaw CR, Campbell ID, Roberts GC, Critchley DR, Barsukov IL (Sep 2008). "Structural basis for the interaction between the cytoplasmic domain of the hyaluronate receptor layilin and the talin F3 subdomain". Journal of Molecular Biology. 382 (1): 112–26. doi:10.1016/j.jmb.2008.06.087. PMID   18638481.
  44. ↑ Salgia R, Sattler M, Pisick E, Li JL, Griffin JD (Feb 1996). "p210BCR/ABL induces formation of complexes containing focal adhesion proteins and the protooncogene product p120c-Cbl". Experimental Hematology. 24 (2): 310–3. PMID   8641358.
  45. ↑ Mazaki Y, Hashimoto S, Sabe H (Mar 1997). "Monocyte cells and cancer cells express novel paxillin isoforms with different binding properties to focal adhesion proteins". The Journal of Biological Chemistry. 272 (11): 7437–44. doi: 10.1074/jbc.272.11.7437 . PMID   9054445.
  46. ↑ Salgia R, Li JL, Lo SH, Brunkhorst B, Kansas GS, Sobhany ES, Sun Y, Pisick E, Hallek M, Ernst T (Mar 1995). "Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210BCR/ABL". The Journal of Biological Chemistry. 270 (10): 5039–47. doi: 10.1074/jbc.270.10.5039 . PMID   7534286.
  47. ↑ Ling K, Doughman RL, Firestone AJ, Bunce MW, Anderson RA (Nov 2002). "Type I gamma phosphatidylinositol phosphate kinase targets and regulates focal adhesions". Nature. 420 (6911): 89–93. Bibcode:2002Natur.420...89L. doi:10.1038/nature01082. PMID   12422220. S2CID   4301885.
  48. ↑ Di Paolo G, Pellegrini L, Letinic K, Cestra G, Zoncu R, Voronov S, Chang S, Guo J, Wenk MR, De Camilli P (Nov 2002). "Recruitment and regulation of phosphatidylinositol phosphate kinase type 1 gamma by the FERM domain of talin". Nature. 420 (6911): 85–9. Bibcode:2002Natur.420...85D. doi:10.1038/nature01147. PMID   12422219. S2CID   1746983.
  49. ↑ Sun N, Critchley DR, Paulin D, Li Z, Robson RM (May 2008). "Identification of a repeated domain within mammalian alpha-synemin that interacts directly with talin". Experimental Cell Research. 314 (8): 1839–49. doi:10.1016/j.yexcr.2008.01.034. PMID   18342854.

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