CLIP-50 immunolocalization during mouse spermiogenesis suggests a role in shaping the sperm nucleus.

Abstract:

:The spermatid nucleus and cytoplasm undergo dramatic morphological modifications during spermatid differentiation into mature sperm. Some of the external force causing this nuclear shaping is generated by a microtubular structure termed the manchette, which attaches to the perinuclear ring of the spermatid. Here, we report the isolation and characterization of a protein component of this perinuclear ring in an immunological screening of a mouse testis cDNA library. We termed this protein CLIP-50 because of its high similarity at the amino acid level to the C-terminal region of the microtubule-binding protein CLIP-170/restin. CLIP-50 lacks the characteristic microtubule-binding motif, but retains a portion of the predicted coiled-coiled domain and the metal-binding motif. The CLIP-50 transcript and protein are abundant in testis. The protein is also expressed in heart, lung, kidney, and skin. A distinct size variant exists in brain. In the spermatids, CLIP-50 protein localizes specifically to the centriolar region where the sperm tail originates and to the perinuclear ring from which the manchette emerges. CLIP-50 staining is retained in the ring throughout its migration over the surface of the nucleus which accompanies the nuclear shaping into its characteristic sperm configuration. This localization pattern indicates a very specific function for this novel CLIP derivative during mouse spermiogenesis.

journal_name

Dev Biol

journal_title

Developmental biology

authors

Tarsounas M,Pearlman RE,Moens PB

doi

10.1006/dbio.2001.0286

subject

Has Abstract

pub_date

2001-08-15 00:00:00

pages

400-10

issue

2

eissn

0012-1606

issn

1095-564X

pii

S0012-1606(01)90286-6

journal_volume

236

pub_type

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