4.1N-Mediated Interactions and Functions in Nerve System and Cancer

Qin Yang; Jing Liu; Zi Wang

doi:10.3389/fmolb.2021.711302

4.1N-Mediated Interactions and Functions in Nerve System and Cancer

Front Mol Biosci. 2021 Sep 13:8:711302. doi: 10.3389/fmolb.2021.711302. eCollection 2021.

Authors

Qin Yang^{1

2}, Jing Liu¹, Zi Wang¹

Affiliations

¹ Molecular Biology Research Center & Center for Medical Genetics, School of Life Sciences, Central South University, Changsha, China.
² School of Medical Laboratory, Shao Yang University, Shaoyang, China.

Abstract

Scaffolding protein 4.1N is a neuron-enriched 4.1 homologue. 4.1N contains three conserved domains, including the N-terminal 4.1-ezrin-radixin-moesin (FERM) domain, internal spectrin-actin-binding (SAB) domain, and C-terminal domain (CTD). Interspersed between the three domains are nonconserved domains, including U1, U2, and U3. The role of 4.1N was first reported in the nerve system. Then, extensive studies reported the role of 4.1N in cancers and other diseases. 4.1N performs numerous vital functions in signaling transduction by interacting, locating, supporting, and coordinating different partners and is involved in the molecular pathogenesis of various diseases. In this review, recent studies on the interactions between 4.1N and its contactors (including the α7AChr, IP3R1, GluR1/4, GluK1/2/3, mGluR8, KCC2, D2/3Rs, CASK, NuMA, PIKE, IP6K2, CAM 1/3, βII spectrin, flotillin-1, pp1, and 14-3-3) and the 4.1N-related biological functions in the nerve system and cancers are specifically and comprehensively discussed. This review provides critical detailed mechanistic insights into the role of 4.1N in disease relationships.

Keywords: 4.1N; CTD; FERM; SAB; cancer 2; nerve system.

Publication types

Review