Structural Comparison of Tektins and Evidence for Their Determination of Complex Spacings in Flagellar Microtubules

Norrander, Jan M.; Perrone, Catherine A.; Amos, Linda; Linck, Richard W.

doi:10.1006/jmbi.1996.0170

Cited by 77 publications

(103 citation statements)

References 42 publications

Supporting

Mentioning

102

Contrasting

Unclassified

Order By: Relevance

“…One idea is that I1 interacts with an intrinsic component of the outer doublet that establishes the 96-nm repeat structure that governs placement of the inner dynein arms, radial spokes, and DRC. Proteins that might be part of such a complex could include the tektins [Norrander et al, 1996;Yanagisawa and Kamiya, 2004;Setter et al, 2006]. Consistent with this idea, tektins may act as a molecular ruler that defines the axonemal 96-nm repeat [Setter et al, 2006] and in Chlamydomonas, defects in tektin assembly are associated with defective inner dynein arm assembly [Yanagisawa and Kamiya, 2004].…”

Section: I1-dynein Mutants Reveal New Features Of Assembly and Dockingmentioning

confidence: 85%

Keeping an eye on I1: I1 dynein as a model for flagellar dynein assembly and regulation

Wirschell

Hendrickson

Sale

2007

Cell Motil. Cytoskeleton

109

View full text Add to dashboard Cite

Among the major challenges in understanding ciliary and flagellar motility is to determine how the dynein motors are assembled and localized and how dyneindriven outer doublet microtubule sliding is controlled. Diverse studies, particularly in Chlamydomonas, have determined that the inner arm dynein I1 is targeted to a unique structural position and is critical for regulating the microtubule sliding required for normal ciliary/flagellar bending. As described in this review, I1 dynein offers additional opportunities to determine the principles of assembly and targeting of dyneins to cellular locations and for studying the mechanisms that regulate dynein activity and control of motility by phosphorylation. Cell Motil.

show abstract

Section: I1-dynein Mutants Reveal New Features Of Assembly and Dockingmentioning

confidence: 85%

Keeping an eye on I1: I1 dynein as a model for flagellar dynein assembly and regulation

Wirschell

Hendrickson

Sale

2007

Cell Motil. Cytoskeleton

109

View full text Add to dashboard Cite

show abstract

“…Tektins A, B, and C are stable protofilament components of biochemically fractionated sea urchin sperm flagella (10,11,22). Tektins are found in the axonemes of flagella, which are composed of heterodimers of tubulins ␣ and ␤ (31), dynein (5,17), and other components (24).…”

mentioning

confidence: 99%

Mice Deficient in the Axonemal Protein Tektin-t Exhibit Male Infertility and Immotile-Cilium Syndrome Due to Impaired Inner Arm Dynein Function

Tanaka

Iguchi

Toyama

et al. 2004

Molecular and Cellular Biology

160

122

View full text Add to dashboard Cite

The haploid germ cell-specific Tektin-t protein is a member of the Tektin family of proteins that form filaments in flagellar, ciliary, and axonemal microtubules. To investigate the physiological role of Tektin-t, we generated mice with a mutation in the tektin-t gene. The homozygous mutant males were infertile, while the females were fully fertile. Sperm morphology and function were abnormal, with frequent bending of the sperm flagella and marked defects in motility. In vitro fertilization assays showed that the defective spermatozoa were able to fertilize eggs. Electron microscopic examination showed that the dynein inner arm structure was disrupted in the sperm flagella of tektin-t-deficient mice. Furthermore, homozygous mutant mice had functionally defective tracheal cilia, as evidenced by altered dynein arm morphology. These results indicate that Tektin-t participates in dynein inner arm formation or attachment and that the loss of Tektin-t results in impaired motility of both flagella and cilia. Therefore, the tektin-t gene is one of the causal genes for immotilecilium syndrome/primary ciliary dyskinesia.

show abstract

“…It is probable that, after filament formation by homo-or hetero dimerization (Setter et al 2006;Norrander et al 1996), TEKTs might play roles as adhesive molecules to integrate ODF, mitochondria and SMR into the peri-axoneme structure in the middle piece of flagella.…”

Section: Discussionmentioning

confidence: 99%

Molecular Cloning and Subcellular Localization of Tektin2-Binding Protein 1 (Ccdc 172) in Rat Spermatozoa

Yamaguchi

Kaneko

Inai

et al. 2014

J Histochem Cytochem.

View full text Add to dashboard Cite

SummaryTektins (TEKTs) are composed of a family of filament-forming proteins localized in cilia and flagella. Five types of mammalian TEKTs have been reported, all of which have been verified to be present in sperm flagella. TEKT2, which is indispensable for sperm structure, mobility, and fertilization, was present at the periphery of the outer dense fiber (ODF) in the sperm flagella. By yeast two-hybrid screening, we intended to isolate flagellar proteins that could interact with TEKT2, which resulted in the isolation of novel two genes from the mouse testis library, referred as a TEKT2-binding protein 1 (TEKT2BP1) and -protein 2 (TEKT2BP2). In this study, we characterized TEKT2BP1, which is registered as a coiled-coil domain-containing protein 172 (Ccdc172) in the latest database. RT-PCR analysis indicated that TEKT2BP1 was predominantly expressed in rat testis and that its expression was increased after 3 weeks of postnatal development. Immunocytochemical studies discovered that TEKT2BP1 localized in the middle piece of rat spermatozoa, predominantly concentrated at the mitochondria sheath of the flagella. We hypothesize that the TEKT2-TEKT2BP1 complex might be involved in the structural linkage between the ODF and mitochondria in the middle piece of the sperm flagella. (J Histochem Cytochem 62:286-297, 2014) Keywords Tektin2, TEKT2BP1 (Ccdc172), spermatozoon, flagellum, peri-axoneme structure

show abstract

Structural Comparison of Tektins and Evidence for Their Determination of Complex Spacings in Flagellar Microtubules

Cited by 77 publications

References 42 publications

Keeping an eye on I1: I1 dynein as a model for flagellar dynein assembly and regulation

Keeping an eye on I1: I1 dynein as a model for flagellar dynein assembly and regulation

Mice Deficient in the Axonemal Protein Tektin-t Exhibit Male Infertility and Immotile-Cilium Syndrome Due to Impaired Inner Arm Dynein Function

Molecular Cloning and Subcellular Localization of Tektin2-Binding Protein 1 (Ccdc 172) in Rat Spermatozoa

Contact Info

Product

Resources

About