embryonic tissues. Curr Top Dev Biol
130:245–274
7. Hoffman BD, Grashoff C, Schwartz MA
(2011) Dynamic molecular processes mediate
cellular
mechanotransduction.
Nature
475:316–323
8. Depoil D, Dustin ML (2014) Force and affinity in ligand discrimination by the TCR.
Trends Immunol 35:597–603
9. Chen W, Lou J, Evans EA, Zhu C (2012)
Observing force-regulated conformational
changes and ligand dissociation from a single
integrin on cells. J Cell Biol 199:497–512
10. Hu X, Margadant FM, Yao M, Sheetz MP
(2017) Molecular stretching modulates
mechanosensing pathways: molecular stretching modulates mechanosensing pathways.
Protein Sci 26:1337–1351
11. Pannekoek W-J, de Rooij J, Gloerich M
(2019) Force transduction by cadherin adhesions in morphogenesis. F1000Res 8:1044
12. Cailliez F, Lavery R (2005) Cadherin
mechanics and complexation: the importance
of calcium binding. Biophys J 89:3895–3903
13. Springer TA, Dustin ML (2012) Integrin
inside-out signaling and the immunological
synapse. Curr Opin Cell Biol 24:107–115
14. Rutherford SL, Zuker CS (1994) Protein
folding and the regulation of signaling pathways. Cell 79:1129–1132
15. Papagrigoriou E, Gingras AR, Barsukov IL,
Bate N, Fillingham IJ, Patel B, Frank R, Ziegler WH, Roberts GC, Critchley DR, Emsley J
(2004) Activation of a vinculin-binding site in
the talin rod involves rearrangement of a fivehelix bundle. EMBO J 23:2942–2951
16. Smith ML, Gourdon D, Little WC, Kubow
KE, Eguiluz RA, Luna-Morris S, Vogel V
(2007) Force-induced unfolding of fibronectin in the extracellular matrix of living cells.
PLoS Biol 5:e268
17. Manjunath GP, Ramanujam PL, Galande S
(2018) Structure function relations in PDZdomain-containing proteins: implications for
protein networks in cellular signalling. J Biosci
43:155–171
18. Lee H-J, Zheng JJ (2010) PDZ domains and
their binding partners: structure, specificity,
and modification. Cell Commun Signal 8:8
19. Charras G, Yap AS (2018) Tensile forces and
mechanotransduction at cell–cell junctions.
Curr Biol 28:R445–R457
20. Heinemann U, Schuetz A (2019) Structural
features of tight-junction proteins. Int J Mol
Sci 20:6020
21. Stevenson BR, Siliciano JD, Mooseker MS,
Goodenough DA (1986) Identification of
ZO-1: a high molecular weight polypeptide
associated with the tight junction (zonula
occludens) in a variety of epithelia. J Cell
Biol 103:755–766
22. Fanning AS, Jameson BJ, Jesaitis LA, Anderson JM (1998) The tight junction protein
ZO-1 establishes a link between the transmembrane protein occludin and the actin
cytoskeleton. J Biol Chem 273:29745–29753
23. Itoh M, Nagafuchi A, Moroi S, Tsukita S
(1997) Involvement of ZO-1 in cadherinbased cell adhesion through its direct binding
to α catenin and actin filaments. J Cell Biol
138:181–192
24. Itoh M, Furuse M, Morita K, Kubota K,
Saitou M, Tsukita S (1999) Direct binding
of three tight junction-associated Maguks,
Zo-1, Zo-2, and Zo-3, with the Cooh termini
of claudins. J Cell Biol 147:1351–1363
25. Wittchen ES, Haskins J, Stevenson BR (1999)
Protein interactions at the tight junction.
Actin has multiple binding partners, and
ZO-1 forms independent complexes with
ZO-2
and
ZO-3.
J
Biol
Chem
274:35179–35185
26. Remue E, Meerschaert K, Oka T,
Boucherie C, Vandekerckhove J, Sudol M,
Gettemans J (2010) TAZ interacts with
zonula occludens-1 and -2 proteins in a
PDZ-1 dependent manner. FEBS Lett
584:4175–4180
27. Balda MS, Matter K (2000) The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression.
EMBO J 19:2024–2033
28. Spadaro D, Tapia R, Jond L, Sudol M, Fanning AS, Citi S (2014) ZO proteins redundantly regulate the transcription factor
DbpA/ZONAB.
J
Biol
Chem
289:22500–22511
29. Balda MS, Garrett MD, Matter K (2003) The
ZO-1-associated Y-box factor ZONAB regulates epithelial cell proliferation and cell density. J Cell Biol 160:423–432
30. Sourisseau T, Georgiadis A, Tsapara A, Ali
RR, Pestell R, Matter K, Balda MS (2006)
Regulation of PCNA and cyclin D1 expression and epithelial morphogenesis by the
ZO-1-regulated
transcription
factor
ZONAB/DbpA.
Mol
Cell
Biol
26:2387–2398
31. Spadaro D, Le S, Laroche T, Mean I, Jond L,
Yan J, Citi S (2017) Tension-dependent
stretching activates ZO-1 to control the
270
Elsa Bazellie ` res and Andre ´ Le Bivic
130:245–274
7. Hoffman BD, Grashoff C, Schwartz MA
(2011) Dynamic molecular processes mediate
cellular
mechanotransduction.
Nature
475:316–323
8. Depoil D, Dustin ML (2014) Force and affinity in ligand discrimination by the TCR.
Trends Immunol 35:597–603
9. Chen W, Lou J, Evans EA, Zhu C (2012)
Observing force-regulated conformational
changes and ligand dissociation from a single
integrin on cells. J Cell Biol 199:497–512
10. Hu X, Margadant FM, Yao M, Sheetz MP
(2017) Molecular stretching modulates
mechanosensing pathways: molecular stretching modulates mechanosensing pathways.
Protein Sci 26:1337–1351
11. Pannekoek W-J, de Rooij J, Gloerich M
(2019) Force transduction by cadherin adhesions in morphogenesis. F1000Res 8:1044
12. Cailliez F, Lavery R (2005) Cadherin
mechanics and complexation: the importance
of calcium binding. Biophys J 89:3895–3903
13. Springer TA, Dustin ML (2012) Integrin
inside-out signaling and the immunological
synapse. Curr Opin Cell Biol 24:107–115
14. Rutherford SL, Zuker CS (1994) Protein
folding and the regulation of signaling pathways. Cell 79:1129–1132
15. Papagrigoriou E, Gingras AR, Barsukov IL,
Bate N, Fillingham IJ, Patel B, Frank R, Ziegler WH, Roberts GC, Critchley DR, Emsley J
(2004) Activation of a vinculin-binding site in
the talin rod involves rearrangement of a fivehelix bundle. EMBO J 23:2942–2951
16. Smith ML, Gourdon D, Little WC, Kubow
KE, Eguiluz RA, Luna-Morris S, Vogel V
(2007) Force-induced unfolding of fibronectin in the extracellular matrix of living cells.
PLoS Biol 5:e268
17. Manjunath GP, Ramanujam PL, Galande S
(2018) Structure function relations in PDZdomain-containing proteins: implications for
protein networks in cellular signalling. J Biosci
43:155–171
18. Lee H-J, Zheng JJ (2010) PDZ domains and
their binding partners: structure, specificity,
and modification. Cell Commun Signal 8:8
19. Charras G, Yap AS (2018) Tensile forces and
mechanotransduction at cell–cell junctions.
Curr Biol 28:R445–R457
20. Heinemann U, Schuetz A (2019) Structural
features of tight-junction proteins. Int J Mol
Sci 20:6020
21. Stevenson BR, Siliciano JD, Mooseker MS,
Goodenough DA (1986) Identification of
ZO-1: a high molecular weight polypeptide
associated with the tight junction (zonula
occludens) in a variety of epithelia. J Cell
Biol 103:755–766
22. Fanning AS, Jameson BJ, Jesaitis LA, Anderson JM (1998) The tight junction protein
ZO-1 establishes a link between the transmembrane protein occludin and the actin
cytoskeleton. J Biol Chem 273:29745–29753
23. Itoh M, Nagafuchi A, Moroi S, Tsukita S
(1997) Involvement of ZO-1 in cadherinbased cell adhesion through its direct binding
to α catenin and actin filaments. J Cell Biol
138:181–192
24. Itoh M, Furuse M, Morita K, Kubota K,
Saitou M, Tsukita S (1999) Direct binding
of three tight junction-associated Maguks,
Zo-1, Zo-2, and Zo-3, with the Cooh termini
of claudins. J Cell Biol 147:1351–1363
25. Wittchen ES, Haskins J, Stevenson BR (1999)
Protein interactions at the tight junction.
Actin has multiple binding partners, and
ZO-1 forms independent complexes with
ZO-2
and
ZO-3.
J
Biol
Chem
274:35179–35185
26. Remue E, Meerschaert K, Oka T,
Boucherie C, Vandekerckhove J, Sudol M,
Gettemans J (2010) TAZ interacts with
zonula occludens-1 and -2 proteins in a
PDZ-1 dependent manner. FEBS Lett
584:4175–4180
27. Balda MS, Matter K (2000) The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression.
EMBO J 19:2024–2033
28. Spadaro D, Tapia R, Jond L, Sudol M, Fanning AS, Citi S (2014) ZO proteins redundantly regulate the transcription factor
DbpA/ZONAB.
J
Biol
Chem
289:22500–22511
29. Balda MS, Garrett MD, Matter K (2003) The
ZO-1-associated Y-box factor ZONAB regulates epithelial cell proliferation and cell density. J Cell Biol 160:423–432
30. Sourisseau T, Georgiadis A, Tsapara A, Ali
RR, Pestell R, Matter K, Balda MS (2006)
Regulation of PCNA and cyclin D1 expression and epithelial morphogenesis by the
ZO-1-regulated
transcription
factor
ZONAB/DbpA.
Mol
Cell
Biol
26:2387–2398
31. Spadaro D, Le S, Laroche T, Mean I, Jond L,
Yan J, Citi S (2017) Tension-dependent
stretching activates ZO-1 to control the
270
Elsa Bazellie ` res and Andre ´ Le Bivic