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Polyubiquitination and Proteasome Signals in Tubulobulbar Complexes of Rat Late Spermatids

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DOI: 10.4236/cellbio.2013.24019    2,772 Downloads   6,312 Views   Citations

ABSTRACT

To illustrate the involvement of tubulobulbar complexes (TBC) in ubiquitin-proteasome degradation of unnecessary proteins in the head cytoplasm of late spermatids, the localization of polyubiquitin and proteasome was studied by immunofluorescence and immunoelectron microscopy. Polyubiquitin localized to TBC and proteasome subunit α to dense materials surrounding the TBC in the cytoplasm of Sertoli cell enwrapping sickle-shaped spermatid heads. The results suggest that the TBC is a structural device for ubiquin-proteasome degradation of unnecessary proteins in the cytoplasm of spermatid head during rapid reduction of the head cytoplasm and nuclear compaction of late spermatids.

Conflicts of Interest

The authors declare no conflicts of interest.

Cite this paper

M. Akashi, S. Yokota and H. Fujita, "Polyubiquitination and Proteasome Signals in Tubulobulbar Complexes of Rat Late Spermatids," CellBio, Vol. 2 No. 4, 2013, pp. 173-178. doi: 10.4236/cellbio.2013.24019.

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