Dual roles of the N-terminal coiled-coil domain of an Aplysia sec7 protein: homodimer formation and nuclear export

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Cytohesin family proteins act as guanine nucleotide exchange factors (GEFs) 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 HEK293T 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 CRM1-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 CRM1-dependent or a CRM1-independent pathway.
Publisher
WILEY-BLACKWELL
Issue Date
2016-12
Language
English
Article Type
Article
Keywords

NUCLEOTIDE EXCHANGE FACTORS; CYTOHESIN/ARNO FAMILY; FACTORS INTERACTS; LOCALIZATION; SIGNALS; BINDING; ASSOCIATION; EXPRESSION; SEQUENCE; DATABASE

Citation

JOURNAL OF NEUROCHEMISTRY, v.139, no.6, pp.1102 - 1112

ISSN
0022-3042
DOI
10.1111/jnc.13875
URI
http://hdl.handle.net/10203/220146
Appears in Collection
BS-Journal Papers(저널논문)
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