Innovation Fund of Hungary, financed under the 2018-1.2.1-NKP
funding scheme. This work was completed in the ELTE Thematic
Excellence Programm 2020 Supperted by the Nation Research,
Development and Innovation Office (TKP2020-IKA-05)
References
1. Loregian A, Palu ` G (2005) Disruption of
protein-protein interactions: towards new targets for chemotherapy. J Cell Physiol
204:750–762. https://doi.org/10.1002/jcp.
20356
2. Vidal M, Cusick ME, Baraba ´si AL (2011)
Interactome networks and human disease.
Cell
144:986–998.
https://doi.org/10.
1016/j.cell.2011.02.016
3. Nishi H, Hashimoto K, Panchenko AR (2011)
Phosphorylation in protein-protein binding:
effect on stability and function. Structure
19:1807–1815. https://doi.org/10.1016/j.
str.2011.09.021
4. Landry CR, Freschi L, Zarin T, Moses AM
(2014) Turnover of protein phosphorylation
evolving under stabilizing selection. Front
Genet 5:1–6. https://doi.org/10.3389/
fgene.2014.00245
5. Van Roey K, Uyar B, Weatheritt RJ, Dinkel H,
Seiler M, Budd A, Gibson TJ, Davey NE
(2014) Short linear motifs: ubiquitous and
functionally diverse protein interaction modules directing cell regulation. Chem Rev
114:6733–6778. https://doi.org/10.1021/
cr400585q
6. Lee HJ, Zheng JJ (2010) PDZ domains and
their binding partners: structure, specificity,
and modification. Cell Commun Signal
8:1–18.
https://doi.org/10.1186/1478811X-8-8
7. Luck K, Charbonnier S, Trave ´ G (2012) The
emerging contribution of sequence context to
the specificity of protein interactions mediated
by PDZ domains. FEBS Lett 586:2648–2661.
https://doi.org/10.1016/j.febslet.2012.03.
056
8. Nourry C, Grant SGN, Borg JP (2003) PDZ
domain proteins: plug and play! Sci STKE
2003:1–13
9. Go ´ gl G, Biri-Kova ´cs B, Po ´ti A ´ L, Vada ´szi H,
Szeder B, Bodor A, Schlosser G, A ´ cs A,
Turia ´k L, Buday L, Alexa A, Nyitray L, Reme ´nyi A (2018) Dynamic control of RSK complexes by phosphoswitch-based regulation.
FEBS J 285:46–71. https://doi.org/10.
1111/febs.14311
10. Sundell
GN,
Arnold
R,
Ali
M,
Naksukpaiboon P, Orts J, Gu ¨ntert P, Chi CN,
Ivarsson Y (2018) Proteome-wide analysis of
phosphor-regulated PDZ domain interactions.
Mol Syst Biol 14:1–22. https://doi.org/10.
15252/msb.20178129
11. Nishi H, Shaytan A, Panchenko AR (2014)
Physicochemical mechanisms of protein regulation by phosphorylation. Front Genet
5:1–10.
https://doi.org/10.3389/fgene.
2014.00270
12. Pawson T (2004) Specificity in signal transduction: from phosphotyrosine-SH2 domain
interactions to complex cellular systems. Cell
116:191–203.
https://doi.org/10.1016/
S0092-8674(03)01077-8
13. Pedersen SW, Albertsen L, Moran GE,
Levesque B, Pedersen SB, Bartels L,
Wapenaar H, Ye F, Zhang M, Bowen ME,
Strømgaard K (2017) Site-specific phosphorylation of PSD-95 PDZ domains reveals finetuned regulation of protein-protein interactions. ACS Chem Biol 12:2313–2323.
https://doi.org/10.1021/acschembio.
7b00361
14. Go ´ gl G, Biri-Kova ´cs B, Durbesson F, Jane P,
Nomine Y, Kostmann C, Bilics V, Simon M,
Reme ´nyi A, Vincentelli R, Trave G, Nyitray L
(2019) Rewiring of RSK–PDZ interactome by
linear motif phosphorylation. J Mol Biol
431:1234–1249. https://doi.org/10.1016/j.
jmb.2019.01.038
15. Vincentelli R, Luck K, Poirson J et al (2015)
Quantifying domain-ligand affinities and specificities by high-throughput holdup assay. Nat
Methods 12:787–793. https://doi.org/10.
1038/nmeth.3438
16. Mortier E, Wuytens G, Leenaerts I, Hannes F,
Heung MY, Degeest G, David G, Zimmermann P (2005) Nuclear speckles and nucleoli
targeting by PIP2-PDZ domain interactions.
EMBO J 24:2556–2565. https://doi.org/10.
1038/sj.emboj.7600722
17. Gianni S, Walma T, Arcovito A, Calosci N,
Bellelli A, Engstro ¨m A, Travaglini-Allocatelli C,
Brunori M, Jemth P, Vuister GW (2006) Demonstration of long-range interactions in a PDZ
domain by NMR, kinetics, and protein engineering. Structure 14:1801–1809. https://
doi.org/10.1016/j.str.2006.10.010
Regulation of RSK1-PDZ Domain Interactions
191
funding scheme. This work was completed in the ELTE Thematic
Excellence Programm 2020 Supperted by the Nation Research,
Development and Innovation Office (TKP2020-IKA-05)
References
1. Loregian A, Palu ` G (2005) Disruption of
protein-protein interactions: towards new targets for chemotherapy. J Cell Physiol
204:750–762. https://doi.org/10.1002/jcp.
20356
2. Vidal M, Cusick ME, Baraba ´si AL (2011)
Interactome networks and human disease.
Cell
144:986–998.
https://doi.org/10.
1016/j.cell.2011.02.016
3. Nishi H, Hashimoto K, Panchenko AR (2011)
Phosphorylation in protein-protein binding:
effect on stability and function. Structure
19:1807–1815. https://doi.org/10.1016/j.
str.2011.09.021
4. Landry CR, Freschi L, Zarin T, Moses AM
(2014) Turnover of protein phosphorylation
evolving under stabilizing selection. Front
Genet 5:1–6. https://doi.org/10.3389/
fgene.2014.00245
5. Van Roey K, Uyar B, Weatheritt RJ, Dinkel H,
Seiler M, Budd A, Gibson TJ, Davey NE
(2014) Short linear motifs: ubiquitous and
functionally diverse protein interaction modules directing cell regulation. Chem Rev
114:6733–6778. https://doi.org/10.1021/
cr400585q
6. Lee HJ, Zheng JJ (2010) PDZ domains and
their binding partners: structure, specificity,
and modification. Cell Commun Signal
8:1–18.
https://doi.org/10.1186/1478811X-8-8
7. Luck K, Charbonnier S, Trave ´ G (2012) The
emerging contribution of sequence context to
the specificity of protein interactions mediated
by PDZ domains. FEBS Lett 586:2648–2661.
https://doi.org/10.1016/j.febslet.2012.03.
056
8. Nourry C, Grant SGN, Borg JP (2003) PDZ
domain proteins: plug and play! Sci STKE
2003:1–13
9. Go ´ gl G, Biri-Kova ´cs B, Po ´ti A ´ L, Vada ´szi H,
Szeder B, Bodor A, Schlosser G, A ´ cs A,
Turia ´k L, Buday L, Alexa A, Nyitray L, Reme ´nyi A (2018) Dynamic control of RSK complexes by phosphoswitch-based regulation.
FEBS J 285:46–71. https://doi.org/10.
1111/febs.14311
10. Sundell
GN,
Arnold
R,
Ali
M,
Naksukpaiboon P, Orts J, Gu ¨ntert P, Chi CN,
Ivarsson Y (2018) Proteome-wide analysis of
phosphor-regulated PDZ domain interactions.
Mol Syst Biol 14:1–22. https://doi.org/10.
15252/msb.20178129
11. Nishi H, Shaytan A, Panchenko AR (2014)
Physicochemical mechanisms of protein regulation by phosphorylation. Front Genet
5:1–10.
https://doi.org/10.3389/fgene.
2014.00270
12. Pawson T (2004) Specificity in signal transduction: from phosphotyrosine-SH2 domain
interactions to complex cellular systems. Cell
116:191–203.
https://doi.org/10.1016/
S0092-8674(03)01077-8
13. Pedersen SW, Albertsen L, Moran GE,
Levesque B, Pedersen SB, Bartels L,
Wapenaar H, Ye F, Zhang M, Bowen ME,
Strømgaard K (2017) Site-specific phosphorylation of PSD-95 PDZ domains reveals finetuned regulation of protein-protein interactions. ACS Chem Biol 12:2313–2323.
https://doi.org/10.1021/acschembio.
7b00361
14. Go ´ gl G, Biri-Kova ´cs B, Durbesson F, Jane P,
Nomine Y, Kostmann C, Bilics V, Simon M,
Reme ´nyi A, Vincentelli R, Trave G, Nyitray L
(2019) Rewiring of RSK–PDZ interactome by
linear motif phosphorylation. J Mol Biol
431:1234–1249. https://doi.org/10.1016/j.
jmb.2019.01.038
15. Vincentelli R, Luck K, Poirson J et al (2015)
Quantifying domain-ligand affinities and specificities by high-throughput holdup assay. Nat
Methods 12:787–793. https://doi.org/10.
1038/nmeth.3438
16. Mortier E, Wuytens G, Leenaerts I, Hannes F,
Heung MY, Degeest G, David G, Zimmermann P (2005) Nuclear speckles and nucleoli
targeting by PIP2-PDZ domain interactions.
EMBO J 24:2556–2565. https://doi.org/10.
1038/sj.emboj.7600722
17. Gianni S, Walma T, Arcovito A, Calosci N,
Bellelli A, Engstro ¨m A, Travaglini-Allocatelli C,
Brunori M, Jemth P, Vuister GW (2006) Demonstration of long-range interactions in a PDZ
domain by NMR, kinetics, and protein engineering. Structure 14:1801–1809. https://
doi.org/10.1016/j.str.2006.10.010
Regulation of RSK1-PDZ Domain Interactions
191