TY  - GEN
T1  - ZYX-1/Zyxin plays a minor role in oocyte transit through the spermatheca in C. elegans
AU  - Castaneda, Perla G.
AU  - Wu, Nan
AU  - Qiu, Zhongqiang
AU  - Lee, Myeongwoo
AU  - Cram, Erin J.
DO  - 10.17912/micropub.biology.000489
UR  - http://beta.micropublication.org/journals/biology/micropub-biology-000489/
AB  - Zyxin is a LIN-11, Isl1, and MEC-3 (LIM)-domain protein that, in mammalian cells, binds alpha actinin and other cytoskeletal-associated proteins. Zyxin localizes to the integrin-based adhesive structures known as focal adhesions and to stress fibers, which are contractile acto-myosin bundles that regulate cell shape and contractility (Wang et al. 2019). The C. elegans protein ZYX-1, a protein with similarity to zyxin, migfilin, TRIP6, and LPP (Lecroisey et al. 2013), was identified in a screen for binding partners of germline RNA helicase (GLH) proteins (P. Smith et al. 2002). Similar to mammalian zyxin, ZYX-1 contains three LIM domains, a potential nuclear export signal (NES) and three proline rich regions (PRR). ZYX-1 is localized to the dense body/Z-disk in body wall muscle and interacts with DEB-1/vinculin (Lecroisey et al. 2013), ATN-1/α-actinin (Lecroisey et al. 2013) , and DYC-1, a dense-body specific protein that potentially interacts with DYS-1/dystrophin (Lecroisey et al. 2008). ZYX-1 might play a role in signaling between the cytoplasm and the nucleus, as a portion of the ZYX-1 protein is translocated from the cytoplasm to the nucleus (Lecroisey et al. 2013). Mounting evidence in mammalian cells suggests that zyxin is mechanosensitive and re-localizes to stress fibers that are under tension (Wang et al. 2019; M. Smith et al. 2010; Schiller et al. 2011), and participates in the repair of damaged actin fibers (M. Smith et al. 2010). It is not known whether ZYX-1 fulfills a similar function in C. elegans.
PY  - 2021
JO  - microPublication Biology
ER  -