| 2001 |
TLN2 encodes a protein similar in size and sequence to talin1 throughout its length (74% identity, 86% similarity), with conserved intron/exon boundaries (except two), but gives rise to multiple transcripts with highest expression in heart, in contrast to the ubiquitously expressed single ~8-kb talin1 mRNA. |
Genomic database assembly, EST analysis, and sequence comparison |
Biochemical and biophysical research communications |
Medium |
11527381
|
| 2005 |
Mammalian Talin-1 and Talin-2 bind to different protein partners as determined by proteomic analysis, indicating functional divergence following gene duplication early in the chordate lineage. |
Proteomic analysis (protein interaction profiling) |
Gene |
Low |
16216449
|
| 2007 |
Talin2 expression is upregulated during striated muscle differentiation (at both mRNA and protein levels), localizes to costameres and intercalated disks in mature striated muscle (stable adhesion complexes), whereas talin1 localizes to focal adhesions in undifferentiated myoblasts. GFP-Talin2 ectopic expression in myoblasts dysregulates the actin cytoskeleton. |
Isoform-specific antibodies, GFP-tagging and live-cell imaging, C2C12 and primary human myoblast differentiation model, RT-PCR and western blot |
Cell motility and the cytoskeleton |
High |
17183545
|
| 2012 |
In the adult mouse heart, Talin2 is the dominant talin isoform localizing to costameres; global deletion of Tln2 in mice caused no structural or functional cardiac changes because cardiomyocyte Talin1 became upregulated as compensation. Tln2 loss increased integrin activation but reduced β1D-integrin isoform levels by 50%. |
Global Tln2 knockout mouse, cardiac function assessment, western blot, immunofluorescence |
Proceedings of the National Academy of Sciences of the United States of America |
High |
28698364
|
| 2012 |
Combined loss of both CM Talin1 and Talin2 in cardiomyocytes led to cardiac dysfunction by 4 weeks with 100% mortality by 6 months, loss of β1D-integrin and other costameric proteins from cardiomyocytes, compromised membrane integrity, and dilated cardiomyopathy. Transgenic integrin overexpression could not rescue the phenotype. |
Cardiomyocyte-specific double knockout mice, cardiac function assessment, histology, immunofluorescence, western blot |
Proceedings of the National Academy of Sciences of the United States of America |
High |
28698364
|
| 2012 |
Mice with complete deletion of the Tln2 coding sequence are viable and fertile with normal organ weights, displaying only a mildly dystrophic phenotype. Tln2-null mouse embryo fibroblasts show no obvious defects in cell adhesion, migration, or proliferation. |
Complete coding sequence deletion knockin mouse (Tln2(cd)), organ weight measurement, MEF functional assays |
Biochemical and biophysical research communications |
Medium |
22925892
|
| 2012 |
Talin1 is the dominant talin isoform in embryonic cardiomyocytes, whereas Talin2 becomes the main isoform in postnatal cardiomyocytes, localizing to costameres. Cardiomyocyte-specific Tln1 knockout mice show normal basal cardiac structure but blunted hypertrophy, less fibrosis, and improved cardiac function after pressure overload, with strongly blunted acute ERK1/2, p38, Akt, and GSK3 signaling responses. |
Cardiomyocyte-specific Tln1 conditional knockout, pressure overload model, echocardiography, western blot for signaling kinases, immunofluorescence |
The Journal of biological chemistry |
High |
23266827
|
| 2016 |
Talin2 has a much stronger binding to β-integrin tails than talin1. Talin2 localizes at invadopodia and is indispensable for traction force generation and invadopodium-mediated matrix degradation. Ablation of talin2 suppressed traction force and invadopodia formation; re-expression of wild-type talin2 but not talin1 rescued these phenotypes. Replacement of talin2 Ser339 with Cys significantly decreased its binding to β1-integrin tails to levels comparable to talin1, and talin2(S339C) could not rescue traction force or invadopodia in talin2-depleted cells. |
siRNA knockdown, traction force microscopy, invadopodium assay, matrix degradation assay, rescue experiments with wild-type and mutant talin2, integrin-binding assay |
Journal of cell science |
High |
27694340
|
| 2017 |
Talin2 S339 forms a hydrogen bond with E353, which is critical for inducing key hydrogen bonds between talin2 N326 and β1-integrin R760, and between talin2 K327 and β1-integrin D759, explaining talin2's higher affinity for β1-integrin relative to talin1. Mutation of talin2 S339L (causing Fifth Finger Camptodactyly) completely disrupted binding to β-integrin tails; substitution of talin1 C336 with Ser enhanced talin1 affinity whereas S339C substitution in talin2 diminished its affinity. |
Integrin-binding affinity assays, site-directed mutagenesis, computational molecular modeling |
Scientific reports |
Medium |
28155884
|
| 2016 |
Exome sequencing identified a missense variant c.1016C>T (p.S339L) in TLN2 co-segregating with Fifth Finger Camptodactyly in a four-generation Chinese Han family. Expression of wild-type and S339L mutant TLN2 in HEK293 cells showed predominant cytoplasmic localization for both. |
Exome sequencing, Sanger sequencing, co-segregation analysis, HEK293 overexpression with subcellular localization |
PloS one |
Medium |
27223613
|
| 2018 |
WWC1 (KIBRA) and TLN2 co-immunoprecipitate in brain tissue and HEK293 cells, co-localize in brain tissue cells, N2a neuroblastoma, and HeLa cell lines, and co-expression of both genes modulates Tau toxicity in Drosophila eye experiments. |
Co-immunoprecipitation (brain tissue and HEK293), co-localization by immunofluorescence, Drosophila Tau toxicity epistasis assay |
Neurobiology of aging |
Medium |
30201328
|
| 2014 |
miR-126-3p directly targets TLN2 by binding a responsive element within the 3'-UTR, as validated by 3'-UTR reporter assays, with an inverse correlation between miR-126-3p and TLN2 mRNA/protein levels during bovine corpus luteum development. |
3'-UTR luciferase reporter assay, qRT-PCR and western blot of TLN2 during CL developmental stages |
Reproduction in domestic animals |
Medium |
25244588
|
| 2022 |
A TLN2 variant (alongside a TPM1 variant) acts as a genetic suppressor: mouse CRISPR knock-in of both the TLN2 and TPM1 variants rescued the heart beating that is absent in Tpm1-mutant embryos (which normally die early with no heartbeat), with near-term fetuses exhibiting large atrial septal defect. This identifies TLN2 as a myofilament actin-binding protein that can suppress a dominant lethal TPM1 mutation. |
CRISPR knock-in mouse model, cardiac phenotype assessment, patient iPSC-derived cardiomyocytes |
Cell reports. Medicine |
Medium |
35243414
|
| 2025 |
Knockdown of talin2 de-differentiates myofibroblasts, reducing myofibroblast-specific morphology, α-smooth muscle actin content, collagen I content, and the pro-fibrotic secretome. Tln2-/- mice are resistant to bleomycin-induced lung fibrosis and to unilateral ureteral obstruction-induced kidney fibrosis, and talin2 knockdown reverses established bleomycin-induced lung fibrosis. |
siRNA knockdown, Tln2 knockout mouse, bleomycin lung fibrosis model, unilateral ureteral obstruction kidney fibrosis model, α-SMA and collagen I immunofluorescence/western blot, secretome analysis |
Scientific reports |
High |
40410300
|
| 2022 |
TLN2 overexpression inhibited ccRCC cell growth, invasion, and migration in vitro and in vivo, inhibited cell cycle progression, and promoted apoptosis. The anti-tumor function of TLN2 was mechanistically linked to inactivation of the Wnt/β-catenin signaling pathway. |
TLN2 overexpression in ccRCC cells, CCK-8, colony formation, transwell, wound healing assays, xenograft in vivo assay, apoptosis/cell cycle flow cytometry, Wnt/β-catenin pathway reporter/activity assay |
Translational andrology and urology |
Medium |
35242640
|