TLN1 Orthologs

Aliases: talin 1, TLN, TLN1, ILWEQ, KIAA1027

Pfam Domain Structure

From TLN1 (human) - phosphorylation sites added via direct mapping

Members of the TLN1 ortholog set
Human Mouse Rat Chicken Fly Worm
CMKB TLN1 Tln1 Tln1 TLN1 - -
Entrez Gene 7094 21894 313494 395194 - -
Uniprot TLN1_HUMAN TLN1_MOUSE - TLN1_CHICK - -
OMIM 186745 - - - - -
Reagents 9 available 11 available - 5 available - -
Results 4 available 1 available - - - -
References
  1. Abrams CS. Intracellular signaling in platelets. Curr. Opin. Hematol. 2005; 12:401-5 (PubMed)
  2. Burridge K, Mangeat P. An interaction between vinculin and talin. Nature 1984; 308:744-6 (PubMed)
  3. Calderwood DA. Talin controls integrin activation. Biochem. Soc. Trans. 2004; 32:434-7 (PubMed)
  4. Campbell ID, Ginsberg MH. The talin-tail interaction places integrin activation on FERM ground. Trends Biochem. Sci. 2004; 29:429-35 (PubMed)
  5. Cram EJ, Schwarzbauer JE. The talin wags the dog: new insights into integrin activation. Trends Cell Biol. 2004; 14:55-7 (PubMed)
  6. Critchley DR. Biochemical and structural properties of the integrin-associated cytoskeletal protein talin. Annu Rev Biophys 2009; 38:235-54 (PubMed)
  7. Critchley DR. Cytoskeletal proteins talin and vinculin in integrin-mediated adhesion. Biochem. Soc. Trans. 2004; 32:831-6 (PubMed)
  8. Critchley DR. Genetic, biochemical and structural approaches to talin function. Biochem. Soc. Trans. 2005; 33:1308-12 (PubMed)
  9. del Rio A, Perez-Jimenez R, Liu R, Roca-Cusachs P, Fernandez JM, Sheetz MP. Stretching single talin rod molecules activates vinculin binding. Science 2009; 323:638-41 (PubMed)
  10. Franco SJ, Rodgers MA, Perrin BJ, Han J, Bennin DA, Critchley DR, Huttenlocher A. Calpain-mediated proteolysis of talin regulates adhesion dynamics. Nat. Cell Biol. 2004; 6:977-83 (PubMed)
  11. Hemmings L, Rees DJ, Ohanian V, Bolton SJ, Gilmore AP, Patel B, Priddle H, Trevithick JE, Hynes RO, Critchley DR. Talin contains three actin-binding sites each of which is adjacent to a vinculin-binding site. J. Cell. Sci. 1996; 109 ( Pt 11):2715-26 (PubMed)
  12. Horwitz A, Duggan K, Buck C, Beckerle MC, Burridge K. Interaction of plasma membrane fibronectin receptor with talin--a transmembrane linkage. Nature 1986; 320:531-3 (PubMed)
  13. Le Clainche C, Carlier MF. Regulation of actin assembly associated with protrusion and adhesion in cell migration. Physiol. Rev. 2008; 88:489-513 (PubMed)
  14. Lin J, Miller MJ, Shaw AS. The c-SMAC: sorting it all out (or in). J. Cell Biol. 2005; 170:177-82 (Full Text)
  15. Moes M, Rodius S, Coleman SJ, Monkley SJ, Goormaghtigh E, Tremuth L, Kox C, van der Holst PP, Critchley DR, Kieffer N. The integrin binding site 2 (IBS2) in the talin rod domain is essential for linking integrin beta subunits to the cytoskeleton. J. Biol. Chem. 2007; 282:17280-8 (PubMed)
  16. Nayal A, Webb DJ, Horwitz AF. Talin: an emerging focal point of adhesion dynamics. Curr. Opin. Cell Biol. 2004; 16:94-8 (PubMed)
  17. Ratnikov BI, Partridge AW, Ginsberg MH. Integrin activation by talin. J. Thromb. Haemost. 2005; 3:1783-90 (PubMed)
  18. Watanabe N, Bodin L, Pandey M, Krause M, Coughlin S, Boussiotis VA, Ginsberg MH, Shattil SJ. Mechanisms and consequences of agonist-induced talin recruitment to platelet integrin alphaIIbbeta3. J. Cell Biol. 2008; 181:1211-22 (Full Text)
Consortium Results & Data
Results & Data
Ortholog Species Type Description Method Status Source Publications
TLN1 none phosphorylation site Talin Endogenous from human platelet 30 phospho-sites in 95.1% coverage of 2540 aa Ginsberg Ratnikov et al.
TLN1 none structure

Talin rod

X-Ray crystallography

completed Liddington Patel et al.
TLN1 none structure

Talin-rod domain and actin

EM and helical reconstruction

completed Hanein
-
TLN1 none structure

Talin (full length)

X-Ray crystallography

completed Liddington
-
TLN1 none structure

Talin rod 655-911

NMR

completed Critchley Patel et al.
TLN1 none structure

Talin fragments for protein splicing and chemical labeling

Cell-based studies

completed Liddington
-
TLN1 none structure

Talin C-terminal helix required for dimer formation

X-Ray crystallography

completed Critchley Gingras et al., Gingras et al.
TLN1 none structure

Talin head for head-tail binding studies

Calorimetric

completed Liddington
-
TLN1 none structure Talin (Ferm-domain) and Actin EM and helical reconstruction completed Hanein Lee et al.
TLN1 none structure

Vinculin and Talin

Atomic Force Microscope

completed Liddington
-
TLN1 none structure

Talin

2D crystallization on lipid monolayers

completed Taylor
-
TLN1 none structure

Alpha-actinin / beta1-integrin - vinculin 1-258 - talin FERM domain complex

2D crystallization on lipid monolayers

completed Taylor
-
TLN1 none structure

Beta tails as an interaction hub

NMR

completed Campbell Oxley et al.
TLN1 none structure

Talin C-terminal actin binding site (I/LWEQ motif)

NMR

completed Critchley Gingras et al., Goult et al.
TLN1 none structure

Talin FO/F1(1-200)

NMR

completed Critchley Gingras et al.
TLN1 none structure Layilin-talin (196-400) X-Ray crystallography, NMR completed Liddington Wegener et al.
TLN1 none structure PIPKIg -talin (196-400) X-Ray crystallography, NMR completed Liddington de Pereda et al.
TLN1 none structure

Talin -beta3 integrin

X-Ray crystallography, NMR

data available Liddington GarcĂ­a-Alvarez et al., Wegener et al., Calderwood et al.
TLN1 none structure

Talin (C-terminal Actin-binding domain)

EM, SAXS, docking and helical reconstruction

completed Hanein Gingras et al., Bate et al., Goult et al., Goult et al.
TLN1 none structure

Full-length talin and actin

EM and tomography

completed Hanein Goult et al.
TLN1 none structure

Talin-vinculin

2D crystallization on lipid monolayers

completed Taylor
-
Discovery» siRNA migration screen using a wound healing approach
Gene Description     MCF-10A phenotype     Secondary screen Wound Image Morphology Time-lapse
TLN1
Aliases: TLN, ILWEQ
Entrez Gene: 7094
siRNA catalog
talin 1
mRNA: NM_006289
Library: MAR
Classification: cytoskeletal
Focal Adhesion Related: Yes
Final bin: Impaired - HC
SMARTpool bin: Impaired
Avg area: 3.61
Avg Alamar: 0.91
Knockdown %: not done
ERBB2: Impaired
TLN1
Link
TLN1
Link
Impaired E
TLN1
Link
Discovery» siRNA Focal Adhesion Phenotypes
Gene Description High-Res Montage
TLN1
Aliases: TLN, ILWEQ
Entrez Gene: 7094
siRNA catalog
talin 1
mRNA: NM_006289
Library: MAR
TLN1
Link
TLN1
Link
Proteomics» Table 1. Identification and Quantitation of Proteins from Cell Body (CB) and Pseudopodium (PD) fractions
IPI Locus Description CB Spectra CB peptide PD Spectra PD peptide ratio
IPI00298994 TLN1 TALIN 1. 137 49 272 78 1.99
Proteomics» Table 2. Proteins in major organelles and subcellular compartments
IPI Locus Description CB Spectra PD Spectra ratio Location
IPI00298994 TLN1 TALIN 1. 137 272 1.99 cytoskeleton
IPI00298994 TLN1 TALIN 1. 137 272 1.99 cytosol
Discovery» MTLn3 invasive data
Gene mRNA Description Expression Ratio
Tln1
Entrez Gene: 21894
mRNA: AA208883
UniGene: Mm.208601
Talin 1 0.3
Consortium Related Products*
Mice » activity page
Ortholog Species Name Method Phenotype Status Jax Availability Source Publications
TLN1 mouse Talin 1
-
Embryonic lethality at E8.5-9.5 with disorganization of embryos at gastrulation. completed
-
-
Monkley et al.
TLN1 mouse Talin - trophoblast cells
-
Reduced spreading on fibronectin and laminin. completed
-
-
Monkley et al.
Constructs » activity page
Ortholog Species Targets Name Amino Acid Range Portion Protocol Source
TLN1 human Talin / PIPKIg - soluble pET30a-talin 1-2541 Talin-full length, S429D gain-of-function mutant
-
Liddington
TLN1 human Talin / PIPKIg pET30b-talin rod 397-2541 Talin rod available Liddington
TLN1 human Talin / PIPKIg - soluble pET30a-talin 1-2541 Full length Talin available Liddington
TLN1 human Talin / PIPKIg pET151-DTOPO talin 196-889 196-889 Talin FERM F2F3 + part of rod available
-
TLN1 human Talin / PIPKIg - soluble pET30a-talin 1-2541 Talin-full length, S446D gain-of-function mutant
-
Liddington
TLN1 human Talin / PIPKIg - soluble pET30a-talin 1-2541 Talin-full length, S429D/S446D double gain-of-function mutant
-
Liddington
TLN1 human Talin / PIPKIg pGEX-4T-2 1984-2344 Talin VBS3
-
-
TLN1 human Talin / PIPKIg pET-29+ Talin Fragment G (L2094A/I12095A mutant)
-
-
TLN1 human Talin / PIPKIg pGEX-4T-2 2071-2135 Talin's actin-binding domain
-
-
TLN1 mouse Layilin / Talin pET15b-layilin 207-400 Layilin tail+talin F2+F3 fusion protein
-
Liddington
TLN1 mouse Talin / PIPKIg - soluble/great yield pET15b-talin 482-636 482-636 Talin's Vinculin-binding domain (VBS1; 4-helix bundle) available Liddington
TLN1 mouse Talin / PIPKIg - soluble/great yield pET15b-talin 482-655 482-655 Talin's VBS1 (autoinhibited 5-helix bundle) available Liddington
TLN1 mouse Talin / PIPKIg - soluble/great yield pET15b-talin 482-789 482-789 Talin rod fragment available Liddington
TLN1 mouse Talin / PIPKIg - soluble/great yield pET151-DTOPO talin 482-889 482-889 Talin rod fragment available Liddington
TLN1 mouse Talin / PIPKIg - soluble/great yield pET151-DTOPO talin 482-889TTTT 482-889 Talin 482-889 stabilized fragment quadruple mutant (T775V/T809I/T833I/T867V) available Liddington
TLN1 mouse Talin / PIPKIg - soluble/great yield pET15b-talin 755-889 755-889 Talin's Vinculin-binding domain 2 (VBS2) available Liddington
TLN1 mouse Talin / PIPKIg - soluble/great yield pET15b-talin 1647-2541 1647-2541 Talin C-terminal fragment available Liddington
TLN1 mouse Talin / PIPKIg - soluble/good yield pET151-DTOPO talin 1843-1973 1843-1973 Talin VBS2 available Liddington
TLN1 chicken Talin / PIPKIg - soluble/great yield pET15b-His-F2F3short 209-400 Talin F2F3 fused to PIPKIgamma tail
-
Liddington
TLN1 chicken Talin - soluble/ok yield pET15b-His-Talin Head 1-400 Talin Head domain available Liddington
TLN1 chicken Talin - soluble/great yield pET15b-His-F2F3 196-400 Talin FERM domain (F2F3 portion) available Liddington
TLN1 chicken Talin / PIPKIg - soluble/ok yield pMAL-cgx-F3,4 309-405 Talin FERM F3 portion
-
Liddington
TLN1 chicken Talin / PIPKIg - low yield pET15b-His-F3 309-405 Talin FERM F3 portion available Liddington

* The resources presented here are largely those generated by the Consortium. The sidebar provides public databases that complement Consortium activities. For mice and biosensors, a public database is not available and therefore we have attempted to generate a migration related list for your convenience.

Pathways

How many degrees of interaction?

Update
Legend: Legend for CMKB pathways