RT Journal Article
T1 Is IIIG9 a New Protein with Exclusive Ciliary Function? Analysis of Its Potential Role in Cancer and Other Pathologies.
A1 Oviedo, María José
A1 Ramírez, Eder
A1 Cifuentes, Manuel
A1 Farkas, Carlos
A1 Mella, Andy
A1 Bertinat, Romina
A1 Gajardo, Roberto
A1 Ferrada, Luciano
A1 Jara, Nery
A1 De Lima, Isabelle
A1 Martínez, Fernando
A1 Nualart, Francisco
A1 Salazar, Katterine
K1 IIIG9
K1 adherens junctions
K1 ciliopathies
K1 ependymal cells
K1 ependymoma
K1 hydrocephaly
K1 protein phosphatase 1
AB The identification of new proteins that regulate the function of one of the main cellular phosphatases, protein phosphatase 1 (PP1), is essential to find possible pharmacological targets to alter phosphatase function in various cellular processes, including the initiation and development of multiple diseases. IIIG9 is a regulatory subunit of PP1 initially identified in highly polarized ciliated cells. In addition to its ciliary location in ependymal cells, we recently showed that IIIG9 has extraciliary functions that regulate the integrity of adherens junctions. In this review, we perform a detailed analysis of the expression, localization, and function of IIIG9 in adult and developing normal brains. In addition, we provide a 3D model of IIIG9 protein structure for the first time, verifying that the classic structural and conformational characteristics of the PP1 regulatory subunits are maintained. Our review is especially focused on finding evidence linking IIIG9 dysfunction with the course of some pathologies, such as ciliopathies, drug dependence, diseases based on neurological development, and the development of specific high-malignancy and -frequency brain tumors in the pediatric population. Finally, we propose that IIIG9 is a relevant regulator of PP1 function in physiological and pathological processes in the CNS.
YR 2022
FD 2022-10-21
LK http://hdl.handle.net/10668/20937
UL http://hdl.handle.net/10668/20937
LA en
DS RISalud
RD Jul 2, 2025