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Dual roles of the N‐terminal coiled‐coil domain of an Aplysia sec7 protein: homodimer formation and nuclear export
Author(s) -
Jun YongWoo,
Lee SeungHee,
Shim Jaehoon,
Lee JinA,
Lim ChaeSeok,
Kaang BongKiun,
Jang DeokJin
Publication year - 2016
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/jnc.13875
Subject(s) - microbiology and biotechnology , nuclear export signal , guanine nucleotide exchange factor , aplysia , chemistry , hek 293 cells , cytoplasm , biology , signal transduction , biochemistry , cell nucleus , gene , evolutionary biology
Cytohesin family proteins act as guanine nucleotide exchange factors ( GEF s) for the ADP ‐ribosylation factor family of small GTP ‐binding proteins. Aplysia Sec7 (ApSec7), a member of the cytohesin family in Aplysia, plays key roles in neurite outgrowth in Aplysia neurons. Although ApSec7 has a conserved coiled‐coil ( CC ) domain, its role was not clear. In this study, we found that the CC domain of ApSec7 and ARNO /cytohesin 2 are involved in homodimer formation, leading to efficient plasma membrane targeting of ApSec7 and ARNO /cytohesin 2 in HEK 293T cells. Therefore, deletion of the CC domain of ApSec7 and ARNO /cytohesin 2 may result in a loss of dimerization and reduce plasma membrane localization. In addition, the CC domains of ApSec7 and ARNO /cytohesin 2 have partially or fully CRM 1‐dependent nuclear export signals, respectively. Taken together, our results suggest that the CC domain of cytohesin family proteins, including ApSec7 and ARNO /cytohesin 2, has dual roles in intracellular targeting: increased plasma membrane targeting through homodimer formation and nuclear exclusion through either a CRM 1‐dependent or a CRM 1‐independent pathway.