Talin-1 (TLN1)
The protein contains 2541 amino acids for an estimated molecular weight of 269767 Da.
Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts (By similarity). (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.
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| Variant | Description |
|---|---|
| dbSNP:rs2295795 | |
| dbSNP:rs17854239 | |
| dbSNP:rs35642290 |
Biological Process
Axon guidance
Blood coagulation
Cell-cell adhesion
Cell-cell junction assembly
Cell-substrate junction assembly
Cellular protein metabolic process
Cortical actin cytoskeleton organization
Endoplasmic reticulum unfolded protein response
Integrin activation
Integrin-mediated signaling pathway
IRE1-mediated unfolded protein response
Movement of cell or subcellular component
Muscle contraction
Obsolete activation of signaling protein activity involved in unfolded protein response
Obsolete cytoskeletal anchoring at plasma membrane
Platelet activation
Platelet aggregation
Platelet degranulation
Viral process
The reference OMIM entry for this protein is 186745
Talin 1; tln1
Talin; tln
DESCRIPTION
Talin links vinculin (193065) to the integrins, and, thus, the cytoskeleton to extracellular matrix (ECM) receptors. It has a mass of 270 kD and shares 23% N-terminal identity with ezrin (123900), which has similar functions (Rees et al., 1990).GENE FUNCTION
DiPaolo et al. (2002) and Ling et al. (2002) presented evidence that talin, through its FERM domain, interacts with the C-terminal tail of the 90-kD PIP5K1C (606102) isoform. The authors showed that this interaction induces clustering of PIP5K1C and talin at focal adhesions and increases the local production of phosphatidylinositol-4,5-bisphosphate. Mechanical forces on matrix-integrin-cytoskeleton linkages are crucial for cell viability, morphology, and organ function. The production of force depends on the molecular connections from ECM-integrin complexes to the cytoskeleton. The minimal matrix complex causing integrin-cytoskeleton connections is a trimer of fibronectin's (135600) integrin-binding domain FNIII7-10. Jiang et al. (2003) reported a specific molecular slip bond that was repeatedly broken by a force of 2 pN at the cellular loading rate of 60 nm/second; this occurred with single trimer beads but not with the monomer. Talin-1, which binds to integrins and actin filaments in vitro, is required for the 2-pN slip bond and rapid cytoskeleton binding. Furthermore, Jiang et al. (2003) showed that inhibition of fibronectin binding to alpha-v-beta-3 integrin (193210 and 173470) and deletion of beta-3 markedly decreased the 2-pN force peak. They suggested that talin-1 initially forms a molecular slip bond between closely packed fibronectin-integrin complexes and the actin cytoskeleton, which can apply a low level of force to fibronectin until many bonds form or a signal is received to activate a force response. Tadokoro et al. (2003) reported that specific binding of the cytoskeletal protein talin to integrin beta subunit (135630) cytoplasmic tails leads to the conformational rearrangements of integrin extracellular domains that increase their affinity. They found that regulated binding of talin to integrin beta tails is a final common element of cellular signaling cascades that control integrin activation. Hu et al. (2007) developed correlational fluorescent speckle microscopy to measure the coupling of focal adhesion proteins to actin filaments (see 102610). Different classes of focal adhesion structural and regulatory molecules exhibited varying degrees of correlated motions with actin filaments, indicating hierarchical transmission of actin motion through focal adhesions. Interactions between vinculin (193065), talin, and actin filaments appear to constitute a slippage interface between the cytoskeleton and integrins, generating a molecular clutch that is regulated during the morphodynamic transitions of cell migration. Kanchanawong et al. (2010) used 3-dimensional super-resolution fluorescence microscopy to map nanoscale protein organization in focal adhesions. Their results revealed that integrins and actin are vertically separated by an approximately 40-nm focal adhesion core region consisting of multiple protein-specific strata: a membrane-apposed integrin signaling layer containing integrin cytoplasmic tails (see 193210), focal adhesion kinase (600758), and paxillin (602505); an intermediate force-transduction layer containing talin and vinculin; and an uppermost actin-regulatory layer containing zyxin (602002), vasodilator-stimulated p ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 186745 was added.