Formin 1 regulates microtubule and F-actin organization to support spermatid transport during spermatogenesis in the rat testis

Nan Li, Dolores D. Mruk, Elizabeth I. Tang, Will M. Lee, Chris K C WONG, C. Yan Cheng*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)

Abstract

Formin 1 confers actin nucleation by generating long stretches of actin microfilaments to support cell movement, cell shape, and intracellular protein trafficking. Formin 1 is likely involved in microtubule (MT) dynamics due to the presence of a MT binding domain near its N terminus. Here, formin 1 was shown to structurally interact with α-tubulin, the building block of MT, and also end-binding protein 1 (a MT plus [+]-end-binding protein that stabilizes MT) in the testis. Knockdown of formin 1 in Sertoli cells with an established tight junction barrier was found to induce down-regulation of detyrosinated MT (a stabilized form of MT), and disorganization of MTs, in which MTs were retracted from the cell cortical zone, mediated through a loss of MT polymerization and down-regulation of Akt1/2 signaling kinase. An efficient knockdown of formin 1 in the testis reduced the number of track-like structures conferred by MTs and F-actin considerably, causing defects in spermatid and phagosome transport across the seminiferous epithelium. In summary, formin1 maintains MT and F-actin track-like structures to support spermatid and phago some transport across the seminiferous epithelium during spermatogenesis.

Original languageEnglish
Pages (from-to)2894-2908
Number of pages15
JournalEndocrinology
Volume157
Issue number7
DOIs
Publication statusPublished - Jul 2016

Scopus Subject Areas

  • Endocrinology

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