98%
921
2 minutes
20
The actin cytoskeleton has been implicated in the assembly of cilia, but roles of actin-dependent motor proteins in ciliogenesis remain unclear. Myosin heavy chain 10 (MYH10), one of the isoforms of non-muscle myosin II, is known to mediate centrosome reorientation during cell migration. Here we show that MYH10 is required for centriole migration to the apical plasma membrane, which occurs at the onset of ciliogenesis. Knockdown of MYH10 in RPE1 cells caused a reduction in the levels of cortical filamentous actin (F-actin) and its binding protein EZRIN. Moreover, both centriole migration and subsequent cilium assembly were defective in MYH10 depleted cells. We further found that MYH10 influences centrosomal recruitment of IFT88, which is required for the transport of building blocks to the ciliary tip. The role of MYH10 in IFT88 recruitment appears to be indirect in that there is a correlation between centriolar IFT88 levels and centriolar positions along the apical-basal axis during ciliogenesis. Our results indicate that MYH10 contributes to ciliogenesis in RPE1 cells by promoting cortical actin-dependent centriole migration.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1016/j.bbrc.2015.04.028 | DOI Listing |
Cytoskeleton (Hoboken)
July 2025
Kusuma School of Biological Sciences, Indian Institute of Technology Delhi, New Delhi, India.
Optineurin (OPTN), a multifunctional cytosolic protein, is recognized as an autophagy adaptor. Its association with neurodegenerative diseases, like ALS, triggered extensive research. OPTN has been found in intracellular organelles, including the mitochondria, Golgi body, endosomes, microtubules, and the nucleus.
View Article and Find Full Text PDFMol Med
August 2025
Department of Breast and Thyroid Surgery, Chongqing Key Laboratory of Molecular Oncology and Epigenetics, The First Affiliated Hospital of Chongqing Medical University, Chongqing, 400016, China.
Objectives: Triple-negative breast cancer (TNBC) is known for its aggressiveness, which can be attributed to its heterogeneity, metastasis, and invasion capabilities. POC1 centriolar protein homolog A (POC1A), a centriolar protein involved in the formation of stable centrioles, has been associated with both cancer promotion and suppression in various malignant tumors. However, the underlying mechanisms that drive POC1A-induced metastases in TNBC remain to be elucidated.
View Article and Find Full Text PDFJ Cell Biol
August 2025
Department of Cell and Developmental Biology, University of Colorado, Anschutz Medical Campus, Aurora, CO, USA.
Excess centrosomes cause defects in mitosis, cell-signaling, and cell migration, and therefore their assembly is tightly regulated. The divergent Polo kinase, PLK4, controls centriole duplication at the heart of centrosome assembly, and elevated PLK4 levels promote centrosome amplification (CA), a founding event of tumorigenesis. Here, we investigate the transcriptional consequences of elevated PLK4 and find Unkempt (UNK), a gene encoding an RNA-binding protein with roles in mRNA translational regulation, to be one of only two upregulated mRNAs.
View Article and Find Full Text PDFInt J Mol Sci
June 2025
MARGen (Molecular Assisted Reproductiona and Genetics) Clinic, 18006 Granada, Spain.
In addition to the male genome, the fertilizing spermatozoon delivers to the oocyte several factors whose deficiency can cause embryo dysfunction. Sperm oocyte-activating factor, identified as phoshoplipase C zeta (PLCζ), drives oocyte exit from meiotic arrest through a signaling pathway initiated by periodic rises of free cytosolic Ca concentration (calcium oscillations). Sperm centrioles, together with oocyte proteins, form centrosomes that are responsible for aster formation, pronuclear migration, and DNA polarization before nuclear syngamy and subsequent mitotic divisions.
View Article and Find Full Text PDFResults Probl Cell Differ
July 2025
Centro de Química Estrutural, Institute of Molecular Sciences, Faculdade de Ciências, Universidade de Lisboa, Lisbon, Portugal.
The cytoskeleton is conserved throughout the eukaryotic lineage and consists of a complex dynamic network mainly composed of three distinct polymers: microtubules (MTs), actin filaments, and intermediate filaments. MTs are polymers of α/β-tubulin heterodimers, playing a myriad of distinct cellular functions and are the main components of complex structures like the mitotic spindle, cilia, and centrioles. Post-translational modifications (PTMs) regulate the function and increase the complexity of the α/β-tubulin heterodimer pools.
View Article and Find Full Text PDF