Conformational buffering underlies functional selection in intrinsically disordered protein regions

Autor: Nicolás S. González-Foutel, Juliana Glavina, Wade M. Borcherds, Matías Safranchik, Susana Barrera-Vilarmau, Amin Sagar, Alejandro Estaña, Amelie Barozet, Nicolás A. Garrone, Gregorio Fernandez-Ballester, Clara Blanes-Mira, Ignacio E. Sánchez, Gonzalo de Prat-Gay, Juan Cortés, Pau Bernadó, Rohit V. Pappu, Alex S. Holehouse, Gary W. Daughdrill, Lucía B. Chemes

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
instname
Nat Struct Mol Biol
Nature Structural and Molecular Biology
Nature Structural and Molecular Biology, 2022, 29 (8), pp.781-790. ⟨10.1038/s41594-022-00811-w⟩

Many disordered proteins conserve essential functions in the face of extensive sequence variation, making it challenging to identify the mechanisms responsible for functional selection. Here we identify the molecular mechanism of functional selection

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f5686ad3777728c8721b6deba4c2af8
https://api.elsevier.com/content/abstract/scopus_id/85135867846

Small peptides patterned after the N-terminus domain of SNAP25 inhibit SNARE complex assembly and regulated exocytosis

Autor: Elvira Valera, Enrique Pérez-Payá, Clara Blanes-Mira, Luis M. Gutiérrez, Antonio Ferrer-Montiel, Jaime M. Merino, Salvador Viniegra, Gregorio Fernández-Ballester

Publikováno v: Journal of Neurochemistry. 88:124-135

Synthetic peptides patterned after the C-terminus of synaptosomal associated protein of 25 kDa (SNAP25) efficiently abrogate regulated exocytosis. In contrast, the use of SNAP25 N-terminal-derived peptides to modulate SNAP receptors (SNARE) complex a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a10b91df841f0a554cf6324cd105b42d
https://doi.org/10.1046/j.1471-4159.2003.02133.x

Modulation of botulinum neurotoxin A catalytic domain stability by tyrosine phosphorylation

Autor: Antonio Ferrer-Montiel, Rosa Planells-Cases, Cristina Ibañez, Gregorio Fernández-Ballester, Clara Blanes-Mira

Publikováno v: FEBS letters. 578(1-2)

Botulinum neurotoxin A (BoNT A) is a substrate of the Src family of tyrosine kinases. Here, we report that the BoNT A light chain (LC) is phosphorylated in the tyrosine-71 located at N-terminus. Covalent modification of this residue notably increases

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::995b3359dc9b0238fa6728d64fd228fb
https://pubmed.ncbi.nlm.nih.gov/15581628

The tryptophan switch: changing ligand-binding specificity from type I to type II in SH3 domains

Autor: Gregorio Fernández-Ballester, Clara Blanes-Mira, Luis Serrano

Publikováno v: Journal of molecular biology. 335(2)

The ability of certain Src homology 3 (SH3) domains to bind specifically both type I and type II polyproline ligands is perhaps the best characterized, but also the worst understood, example in the family of protein-interaction modules. A detailed an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f42d2cc284dbe630aad83ae7c37323c
https://pubmed.ncbi.nlm.nih.gov/14672668

Thermal stabilization of the catalytic domain of botulinum neurotoxin E by phosphorylation of a single tyrosine residue

Autor: Clara Blanes-Mira, Cristina Ibañez, Enrique Pérez-Payá, Rosa Planells-Cases, Antonio Ferrer-Montiel, Gregorio Fernández-Ballester

Publikováno v: Biochemistry. 40(7)

The catalytic domain of clostridial neurotoxins is a substrate of tyrosine-specific protein kinases. The functional role of tyrosine phosphorylation and also the number and location of its (their) phosphorylation site(s) are yet elusive. We have used

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5d9323cf946ded7af427fefcf6047bd
https://pubmed.ncbi.nlm.nih.gov/11329292