In:
Traffic, Wiley, Vol. 13, No. 2 ( 2012-02), p. 218-233
Abstract:
In vertebrates, the nuclear pore complex ( NPC ), the gate for transport of macromolecules between the nucleus and the cytoplasm, consists of approximately 30 different nucleoporins ( Nup s). The Nup and SUMO E 3‐ligase Nup 358/ Ran BP2 are the major components of the cytoplasmic filaments of the NPC . In this study, we perform a structure–function analysis of Nup 358 and describe its role in nuclear import of specific proteins. In a screen for nuclear proteins that accumulate in the cytoplasm upon Nup 358 depletion, we identified proteins that were able to interact with Nup 358 in a receptor‐independent manner. These included the importin α/β‐cargo DBC ‐1 (deleted in breast cancer 1) and DMAP ‐1 ( DNA methyltransferase 1 associated protein 1). Strikingly, a short N ‐terminal fragment of Nup 358 was sufficient to promote import of DBC ‐1, whereas DMAP ‐1 required a larger portion of Nup 358 for stimulated import. Neither the interaction of RanGAP with Nup 358 nor its SUMO ‐ E 3 ligase activity was required for nuclear import of all tested cargos. Together, Nup 358 functions as a cargo‐ and receptor‐specific assembly platform, increasing the efficiency of nuclear import of proteins through various mechanisms.
Type of Medium:
Online Resource
ISSN:
1398-9219
,
1600-0854
DOI:
10.1111/tra.2012.13.issue-2
DOI:
10.1111/j.1600-0854.2011.01302.x
Language:
English
Publisher:
Wiley
Publication Date:
2012
detail.hit.zdb_id:
2020962-9
SSG:
12
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