Polyubiquitination and Proteasome Signals in Tubulobulbar Complexes of Rat Late Spermatids ()
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.
Share and Cite:
Akashi, M. , Yokota, S. and Fujita, H. (2013) Polyubiquitination and Proteasome Signals in Tubulobulbar Complexes of Rat Late Spermatids.
CellBio,
2, 173-178. doi:
10.4236/cellbio.2013.24019.