[HTML][HTML] A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2

R Mahajan, C Delphin, T Guan, L Gerace, F Melchior - Cell, 1997 - cell.com
R Mahajan, C Delphin, T Guan, L Gerace, F Melchior
Cell, 1997cell.com
We have found that the mammalian Ran GTPase–activating protein RanGAP1 is highly
concentrated at the cytoplasmic periphery of the nuclear pore complex (NPC), where it
associates with the 358-kDa Ran–GTP-binding protein RanBP2. This interaction requires
the ATP-dependent posttranslational conjugation of RanGAP1 with SUMO-1 (for small
ubiquitin-related modifier), a novel protein of 101 amino acids that contains low but
significant homology to ubiquitin. SUMO-1 appears to represent the prototype for a novel …
Abstract
We have found that the mammalian Ran GTPase–activating protein RanGAP1 is highly concentrated at the cytoplasmic periphery of the nuclear pore complex (NPC), where it associates with the 358-kDa Ran–GTP-binding protein RanBP2. This interaction requires the ATP-dependent posttranslational conjugation of RanGAP1 with SUMO-1 (for small ubiquitin-related modifier), a novel protein of 101 amino acids that contains low but significant homology to ubiquitin. SUMO-1 appears to represent the prototype for a novel family of ubiquitin-related protein modifiers. Inhibition of nuclear protein import resulting from antibodies directed at NPC-associated RanGAP1 cannot be overcome by soluble cytosolic RanGAP1, indicating that GTP hydrolysis by Ran at RanBP2 is required for nuclear protein import.
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