Nurit, a novel leucine-zipper protein, expressed uniquely in the spermatid flower-like structure

Erez Feige, Aviva Chen, Benny Motro

Research output: Contribution to journalArticlepeer-review

16 Scopus citations


Spermatozoa formation involves drastic morphological and cellular reconstructions. However, the molecular mechanisms driving this process remain elusive. We describe the cloning of a novel murine spermatid-specific gene, designated nurit, identified in a two-hybrid screen for proteins that binds the Nek1 kinase. Nurit protein harbors a leucine-zipper motif, and two additional coiled-coil regions. The C-terminal coiled-coil domain mediates homodimerization of the protein. Nurit homologues are found in primates, pig and rodents. nurit is transcribed through the elongation stage of the spermatids, but is absent from mature spermatozoa. Interestingly, immunogold electron microscopy revealed that the protein is restricted, from its first detectable appearance, to a unique spermatid organelle called the 'flower-like structure'. The function of this structure is unknown, though it may be involved in transporting proteins designated to be discarded via the residual bodies. Nurit is the first marker of the flower-like structure, and its study may provide an excellent opportunity to dissect the function of this organelle.

Original languageEnglish
Pages (from-to)369-377
Number of pages9
JournalMechanisms of Development
Issue number1-2
StatePublished - Sep 2002

Bibliographical note

Funding Information:
This work was supported by the Israel Cancer Research Fund. We express our gratitude to Poornima Upadhya for Nek1 mutant (kat 2J ) mice, Vera Shinder from the Electron Microscopy Unit at the Weizmann Institute for excellent assistance in the electron microscopy, Jeremy Don for two-hybrid testicular cDNA library, and Phillipa Saunders for supplying us with blocks of TGR26 rat testis. This work was done as part of the Ph.D. thesis of Erez Feige in Bar-Ilan University.


  • Cytoplasmic elimination
  • Flower-like structure
  • Homodimerization
  • Leucine zipper
  • NIMA kinase
  • Nek1 kinase
  • Spermiogenesis
  • Testis


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