Kinesin-13, a microtubule-end depolymerase, has been shown to affect the length of cilia, but its ciliary function is unclear. In Tetrahymena thermophila, kinesin-13 positively regulates the axoneme length, influences the properties of ciliary tubulin, and affects the ciliary dynein-dependent motility.

Dynein light chain 1 (LC1) of the outer arm dynein (OAD) complex associates with the microtubule-binding domain (MTBD) of γ heavy chain inside the complex. LC1 is considered to regulate the OAD activity and ciliary/flagellar motion by modulating γ MTBD's affinity to the B-tubule of the doublet microtubule in the axoneme.

To reveal the molecular systems involved in the division of a cell and its contents during cell proliferation is one of the major subjects in cell biology. Although cytoskeletal organization during mitosis has been well studied, consensus on the molecular basis of amitosis has not been achieved. Here we adapted an immunofluorescence method and investigated the cellular localization of γ-tubulin and microtubules (MTs) in dividing Tetrahymena. Although the macronucleus (Mac) lacks a bipolar spindle, γ-tubulin and MTs are specifically detected in the dividing Mac and show a marked change in the pattern of localization. First, γ-tubulin and MTs appear in whole Mac, then, γ-tubulin gathers at the center of the Mac where the aster-like structure of MTs forms. On Mac expansion, MTs associated with numerous dots of γ-tubulin are reorganized into longitudinally arranged bundles, suggesting that the mutual sliding of each filament and polymerization of MTs may induce Mac expansion. Moreover, normal Mac expansion and equal segregation of the Mac are severely disturbed when γ-tubulin is shut off. We propose that γ-tubulin-mediated MT assembly is required in Mac amitosis of Tetrahymena.

No abstract

The present study was conducted to systematically investigate the optimal viral titer as well as the volume of the adenovirus vector (ADV) that expresses α-actinin-AcGFP in the Z-disks of myocytes in the left ventricle (LV) of mice. An injection of 10 μL ADV at viral titers of 2 to 4 × 1011 viral particles per mL (VP/mL) into the LV epicardial surface consistently expressed α-actinin-AcGFP in myocytes in vivo, with the fraction of AcGFP-expressing myocytes at ~10%. Our analysis revealed that SL was ~1.90-2.15 μm upon heart arrest via deep anesthesia. Likewise, we developed a novel fluorescence labeling method of the T-tubular system by treating the LV surface with CellMask Orange (CellMask). We found that the T-tubular distance was ~2.10-2.25 μm, similar to SL, in the healthy heart in vivo. Therefore, the present high-precision visualization method for the Z-disks or the T-tubules is beneficial to unveiling the mechanisms of myocyte contraction in health and disease in vivo.