The cytosolic carboxypeptidases CCP2 and CCP3 catalyze posttranslational removal of acidic amino acids
Tort Regàs, Olívia (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Tanco, Sebastián Martín (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Rocha, Cecilia (Institut Curie)
Bièche, Ivan (Institut Curie)
Seixas, Cecilia (Universidade Nova de Lisboa. Centro de Estudos de Doenças Crónicas)
Bosc, Christophe (Université de Grenoble. Institut des neurosciences)
Andrieux, Annie (Université de Grenoble. Institut des neurosciences)
Moutin, Marie-Jo (Université de Grenoble. Institut des neurosciences)
Avilés, Francesc Xavier (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Lorenzo Rivera, Julia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Janke, Carsten (Institut Curie)

Fecha:	2014
Resumen:	The posttranslational modification of carboxy-terminal tails of tubulin plays an important role in the regulation of the microtubule cytoskeleton. Enzymes responsible for deglutamylating tubulin have been discovered within a novel family of mammalian cytosolic carboxypeptidases. The discovery of these enzymes also revealed the existence of a range of other substrates that are enzymatically deglutamylated. Only four of six mammalian cytosolic carboxypeptidases had been enzymatically characterized. Here we complete the functional characterization of this protein family by demonstrating that CCP2 and CCP3 are deglutamylases, with CCP3 being able to hydrolyze aspartic acids with similar efficiency. Deaspartylation is a novel posttranslational modification that could, in conjunction with deglutamylation, broaden the range of potential substrates that undergo carboxy-terminal processing. In addition, we show that CCP2 and CCP3 are highly regulated proteins confined to ciliated tissues. The characterization of two novel enzymes for carboxy-terminal protein modification provides novel insights into the broadness of this barely studied process.
Ayudas:	Ministerio de Economía y Competitividad BIO2013-44973-R
Derechos:	Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, i la comunicació pública de l'obra, sempre que no sigui amb finalitats comercials, i sempre que es reconegui l'autoria de l'obra original. No es permet la creació d'obres derivades.
Documento:	Article
Materia:	Cytosolic carboxypeptidases ; CCP2 ; CCP3
Publicado en:	Molecular biology of the cell, Vol. 25, No. 19 (Oct. 2014), p. 3017-27, ISSN 1939-4586

Publicat 24 p, 7.3 MB

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