Bacterial Production of CDKL5 Catalytic Domain: Insights in Aggregation, Internal Translation and Phosphorylation Patterns.


Journal

International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791

Informations de publication

Date de publication:
15 Aug 2024
Historique:
received: 19 06 2024
revised: 09 08 2024
accepted: 13 08 2024
medline: 31 8 2024
pubmed: 31 8 2024
entrez: 29 8 2024
Statut: epublish

Résumé

Cyclin-dependent kinase-like 5 (CDKL5) is a serine/threonine protein kinase involved in human brain development and functioning. Mutations in CDKL5, especially in its catalytic domain, cause a severe developmental condition named CDKL5 deficiency disorder. Nevertheless, molecular studies investigating the structural consequences of such mutations are still missing. The CDKL5 catalytic domain harbors different sites of post-translational modification, such as phosphorylations, but their role in catalytic activity, protein folding, and stability has not been entirely investigated. With this work, we describe the expression pattern of the CDKL5 catalytic domain in

Identifiants

pubmed: 39201578
pii: ijms25168891
doi: 10.3390/ijms25168891
pii:
doi:

Substances chimiques

Protein Serine-Threonine Kinases EC 2.7.11.1
CDKL5 protein, human EC 2.7.11.22
Protein Aggregates 0
Recombinant Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : the University of Pennsylvania Orphan Disease Center CDKL5-20-101-08
ID : CDKL5-20-101-08

Auteurs

Andrea Colarusso (A)

Department of Chemical Sciences, University of Naples Federico II, Complesso Universitario Monte S. Angelo, Via Cintia 4, 80126 Naples, Italy.

Concetta Lauro (C)

Department of Chemical Sciences, University of Naples Federico II, Complesso Universitario Monte S. Angelo, Via Cintia 4, 80126 Naples, Italy.

Luisa Canè (L)

CEINGE Advanced Biotechnologies, Via G. Salvatore 486, 80145 Naples, Italy.
Department of Translational Medical Sciences, University of Naples Federico II, Via Sergio Pansini 5, 80131 Naples, Italy.

Flora Cozzolino (F)

Department of Chemical Sciences, University of Naples Federico II, Complesso Universitario Monte S. Angelo, Via Cintia 4, 80126 Naples, Italy.
CEINGE Advanced Biotechnologies, Via G. Salvatore 486, 80145 Naples, Italy.

Maria Luisa Tutino (ML)

Department of Chemical Sciences, University of Naples Federico II, Complesso Universitario Monte S. Angelo, Via Cintia 4, 80126 Naples, Italy.
Istituto Nazionale Biostrutture e Biosistemi I.N.B.B., Viale Medaglie D'Oro 305, 00136 Roma, Italy.

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Classifications MeSH