Cloning of a cDNA Which Encodes a Novel Ubiquitin-like Protein

Kumar, Sharad; Yoshida, Yoko; Noda, Makoto

doi:10.1006/bbrc.1993.2056

Cited by 127 publications

(88 citation statements)

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“…However, in the developing Drosophila eye discs, Cul3-mediated degradation of Ci155 only partially requires Nedd8 modification (Ou et al, 2002), contrasting with the essential role of Nedd8 in Cul3-governed MB neurite terminal morphogenesis. Nedd8 was originally isolated from neural precursor cells, and its expression is developmentally downregulated (Kumar et al, 1993). Together with the requirement of Nedd8 for multiple aspects of MB development, neddylation of cullin family proteins is likely used repeatedly to govern diverse neuronal developmental processes.…”

Section: Discussionmentioning

confidence: 99%

Requirement of Cul3 for Axonal Arborization and Dendritic Elaboration inDrosophilaMushroom Body Neurons

Zhu¹,

Perez²,

Pan³

et al. 2005

J. Neurosci.

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Section: Discussionmentioning

confidence: 99%

Requirement of Cul3 for Axonal Arborization and Dendritic Elaboration inDrosophilaMushroom Body Neurons

Zhu¹,

Perez²,

Pan³

et al. 2005

J. Neurosci.

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“…The elevation of NEDD8 expression was observed in various human tumor cell lines, such as leukemia, HeLa, K562, and MOLT-4 cells but was low in Raji, SW480, and G361 cells. No appreciable change in the NEDD8 expression was observed during embryonic development of mice, although it was reported to be down-regulated developmentally (Kumar et al, 1993;Kamitani et al, 1997).…”

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confidence: 96%

“…In addition, it is of particular interest that SUMO1 can be conjugated to two Lys residues of I-kB where Ub is linked for proteasomal degradation, indicating that SUMO1 may contribute to negative regulation of the NF-kB signaling pathway (Desterro et al, 1998). Other Ubl proteins, yeast Rub1 and its mammalian homolog NEDD8 that was identi®ed as one of the multiple neural precursor cell-expressed developmentally down-regulated genes (Kumar et al, 1993) were found to be ligated to yeast Cdc53 and human Cul-4A, respectively Osaka et al, 1998), which are members of the family of cullin/Cdc53 proteins functioning as an essential component of a multifunctional Ub-protein ligase E3 complex called SCF (Skp1-Cdc53/Cul-1-F-box protein) (Patton et al, 1998a;Elledge and Harper, 1998;Harper and Elledge, 1999). These ®ndings suggest that Rub1 and NEDD8 are functionally equivalent and that the Rub1/NEDD8-modifying pathway plays a key role in the Ub-mediated pathway with respect to cell-cycle regulation (reviewed in Hochstrasser, 1998).…”

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confidence: 99%

Covalent modification of all members of human cullin family proteins by NEDD8

et al. 1999

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Recently we found that NEDD8, a ubiquitin-like protein, was linked covalently to human cullin-4A (abbreviated Cul-4A) by a new ubiquitin-related pathway that is analogous to but distinct from the ligating system for SUMO1, another ubiquitin-like protein. However, it remained unknown whether the other ®ve members of the family of human cullin/Cdc53 proteins are modi®ed by NEDD8. Here we report that all Hs-Cul family proteins, such as Cul-1, Cul-2, Cul-3, Cul-4B, and Cul-5, in addition to Cul-4A, were modi®ed by covalent attachment of NEDD8 in rabbit reticulocyte lysates. Moreover, by comprehensive Northern-blot analyses, we examined multiple tissue distributions of the messages for all Cul-family proteins, NEDD8, and the NEDD8-ligating system consisting of APP-BP1/hUba3, and hUbc12, which function as E1-and E2-like enzymes, respectively. The expressions of Cul-1, Cul-2, and Cul-3 resembled each other and were apparently correlated to those of NEDD8 and the NEDD8-ligating system in various human cells and tissues. However, the mRNA levels of Cul-4A, Cul-4B, and Cul-5 di ered considerably from each other as well as from other Cul-family proteins. The enhanced expression of all Cul-family proteins except Cul-5 was observed in a variety of tumor cell lines.

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“…Recent work has demonstrated that AXR1 interacts with a second protein called ECR1, to activate the ubiquitin-related protein RUB for conjugation (del Pozo et al 1998). RUB is a member of a conserved family of ubiquitin-related proteins present in fungi, plants, and mammals (NEDD-8) (Kumar et al 1993;Rao-Naik et al 1998). Like ubiquitin, RUB is conjugated to target proteins.…”

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confidence: 99%