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Odf2 interacts with Cep128 to form the subdistal appendage of the centriole.
Cenexin controls centrosome positioning during cell migration by modulating microtubule organization and stability.Cenexin is required for spindle orientation.
Cby plays an important role in organization of both primary and motile cilia in collaboration with Cnx.
Trichoplein controls microtubule anchoring at the centrosome by binding to Odf2 and ninein.
Cdk5 in the centriolar appendages mediates cenexin1 localization and primary cilia formation.
Mouse and rat ODF2 protein homolog sequences and expression are compared.
We propose that hCenexin1 is a critical centrosomal component whose C-terminal extension is required for proper recruitment of Plk1 and other components crucial for normal mitosis.
A splice variant of hODF2 called hCenexin1, but not hODF2 itself, efficiently localizes to somatic centrosomes via a variant-specific C-terminal extension and recruits Plk1 through a Cdc2-dependent phospho-S796 motif within the extension.
The authors developed an Mrkn2 knockout mouse model to study the role of this gene, and found that deletion of Mkrn2 in mice led to male infertility and expression of Odf2, a vital protein in spermatogenesis, was significantly decreased.
the C-terminal region (amino acids 214-638) of Odf2 is required for association with Tssk4; demonstrated the phosphorylation site in Odf2 by Tssk4
Pax6 directly regulates the activity of the Odf2 gene encoding for the appendage-specific protein Odf2 with a role for the assembly of mother centriole.
The presence of multiple splicing variants hints that the function of Odf2 is diversified in such a way that each variant has a distinct role in the complex cellular and developmental processes.
In adult mice, Odf2 expression was marked in the interdental cells, Boettcher cells, the root cells and root cell processes. Fainter expression was also visible in the hair cells of the maculae and cristae
C-terminal region of Odf2 in mice is sufficient for ciliogenesis, the resulting basal bodies lack basal feet; loss of basal feet in ciliated epithelia disrupts polarized organization of apical microtubule lattice without affecting planar cell polarity.
Results document the possible impact of loss of one Odf2 allele on sperm tail structure and function, resulting in a novel sperm tail phenotype.
Odf2 contributes to assorted ciliopathies
Odf2 is indispensable for the formation of distal/subdistal appendages and the generation of primary cilia, but not for other cell-cycle-related centriolar functions.
Knockout of the abundant sperm tail protein, outer dense fiber 2, results in preimplantation lethality.
ODF2 is the main isoform in testicular tissue RT-PCR analyses revealed that isoforms are not restricted to specific tissues
findings show that testicular expression of Odf2 correlates with spermiogenesis and ongoing sperm tail formation thus implicating functional differences between ODF2 and Cenexin.
The outer dense fibers are cytoskeletal structures that surround the axoneme in the middle piece and principal piece of the sperm tail. The fibers function in maintaining the elastic structure and recoil of the sperm tail as well as in protecting the tail from shear forces during epididymal transport and ejaculation. Defects in the outer dense fibers lead to abnormal sperm morphology and infertility. This gene encodes one of the major outer dense fiber proteins. Alternative splicing results in multiple transcript variants. The longer transcripts, also known as 'Cenexins', encode proteins with a C-terminal extension that are differentially targeted to somatic centrioles and thought to be crucial for the formation of microtubule organizing centers.
outer dense fiber of sperm tails 2
, outer dense fiber protein 2
, outer dense fiber of sperm tails protein 2
, cancer/testis antigen 134
, cenexin 1
, outer dense fiber of sperm tails, 84-kD
, sperm tail structural protein
, 84 kDa outer dense fiber protein
, outer dense fiber of sperm tail 2
, sperm outer dense fiber major protein 2
, testis-specific autoantigen