KIF3A tail domain phosphorylation is not required for ciliogenesis in mouse embryonic fibroblasts.

ABSTRACT: Primary cilia are essential signaling organelles that protrude from most cells in the body. Heterodimeric kinesin-2 (KIF3A/KIF3B/KAP3) powers several intracellular transport processes, including intraflagellar transport (IFT), essential for ciliogenesis. A long-standing question is how a motor protein is differentially regulated for specific cargos. Since phosphorylation of the KIF3A tail domain was suggested to regulate the activity of kinesin-2 for ciliogenesis, similarly as for the cytosolic cargo N-Cadherin, we set out to map the phosphosites involved in this regulation. Using well-characterized Kif3a^-/-; Kif3b^-/- mouse embryonic fibroblasts, we performed ciliogenesis rescue assays with a library of phosphomimetic mutants comprising all predicted pho

SUBMITTER: Fasawe AS 

PROVIDER: S-EPMC10884758 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature