The UBX domain: a widespread ubiquitin-like module

Buchberger, Alexander; Howard, Mark J.; Proctor, Mark R.; Bycroft, Mark

doi:10.1006/jmbi.2000.4462

Cited by 135 publications

(138 citation statements)

References 40 publications

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“…Considering that this COOH-terminal fragment of Socius contains the Rndbinding domain and the UBX domain, Socius may serve as an adapter or scaffold protein, linking Rnd GTPases to cytoskeletal regulatory molecules that would bind to the UBX domain of Socius. The UBX domain is an ϳ80-amino-acid residue module that is present typically at the COOH terminus of a variety of eukaryotic proteins and is structurally homologous to ubiquitin (3). However, a number of proteins containing the UBX domain so far appear to be unrelated to ubiquitination processes, and the function of the UBX domain remains unknown.…”

Section: Discussionmentioning

confidence: 99%

Socius Is a Novel Rnd GTPase-Interacting Protein Involved in Disassembly of Actin Stress Fibers

Katoh

Harada

Mori

et al. 2002

Molecular and Cellular Biology

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Rho family small GTPases are key regulators of the actin cytoskeleton in various cell types. The Rnd proteins, Rnd1, Rnd2, and Rnd3/RhoE, have been recently identified as new members of the Rho family of GTPases, and expression of Rnd1 or Rnd3 in fibroblasts causes the disassembly of actin stress fibers and the retraction of the cell body to produce extensively branching cellular processes. Here we have performed a yeast two-hybrid screening by using Rnd1 as bait and identified a novel protein that specifically binds to Rnd GTPases. We named this protein Socius. Socius directly binds to Rnd GTPases through its COOH-terminal region. When transfected into COS-7 cells, Socius is translocated to the cell periphery in response to Rnd1 and Rnd3 and colocalized with the GTPases. While expression of wild-type Socius in Swiss 3T3 fibroblasts has little effect on the actin cytoskeleton, the expression of a membrane-targeted form of Socius, containing a COOHterminal farnesylation motif (Socius-CAAX), induces a dramatic loss of stress fibers. The inhibitory effect of Socius-CAAX on stress fiber formation is enhanced by truncation of its NH 2 terminus. On the other hand, the expression of Socius-CAAX or its NH 2 terminus-truncated form suppresses the Rnd-induced retraction of the cell body and the production of extensively branching cellular processes, although the disassembly of stress fibers is observed. We propose that Socius participates in the Rnd GTPase-induced signal transduction pathways, leading to reorganization of the actin cytoskeleton.

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Section: Discussionmentioning

confidence: 99%

Socius Is a Novel Rnd GTPase-Interacting Protein Involved in Disassembly of Actin Stress Fibers

Katoh

Harada

Mori

et al. 2002

Molecular and Cellular Biology

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“…The UBX domain is a module comprising approximately 80 amino acids and displays a b-grasp fold (b-b-a-b-b-a-b) closely resembling the structure of ubiquitin [45]. UBX domain containing proteins constitute the largest family of p97 cofactors [46,47].…”

Section: Ubx and Ubxl Domainsmentioning

confidence: 99%

“…These four residues form the highly conserved R. . .FPR signature motif of UBX proteins [45]. The UBX domain inserts its S3/S4 loop into the hydrophobic cleft separating the two subdomains of the N domain, which represents a binding pocket common to the UBX and UBXL (see below) domains.…”

Section: Ubx and Ubxl Domainsmentioning

confidence: 99%

Control of p97 function by cofactor binding

2015

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Edited by Wilhelm JustKeywords: ATPases Associated with diverse cellular Activities p47 UFD1-NPL4 UBXD1 Inclusion Body Myopathy with Pagets disease of the bone and Fronto-temporal Dementia a b s t r a c t p97 (also known as Cdc48, Ter94, and VCP) is an essential, abundant and highly conserved ATPase driving the turnover of ubiquitylated proteins in eukaryotes. Even though p97 is involved in highly diverse cellular pathways and processes, it exhibits hardly any substrate specificity on its own. Instead, it relies on a large number of regulatory cofactors controlling substrate specificity and turnover. The complexity as well as temporal and spatial regulation of the interactions between p97 and its cofactors is only beginning to be understood at the molecular level. Here, we give an overview on the structural framework of p97 interactions with its cofactors, the emerging principles underlying the assembly of complexes with different cofactors, and the pathogenic effects of disease-associated p97 mutations on cofactor binding.

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“…Members of the largest family of Cdc48 cofactors are related by the UBX (ubiquitin regulatory X) domain; there are seven UBX proteins in Saccharomyces cerevisiae. Structural determination of the UBX domain, which binds specifically to the Cdc48 N-terminal domain (16), revealed a ␤-grasp fold similar to that of ubiquitin (17).…”

mentioning

confidence: 99%

A Conserved Protein with AN1 Zinc Finger and Ubiquitin-like Domains Modulates Cdc48 (p97) Function in the Ubiquitin-Proteasome Pathway

Sá-Moura

Funakoshi

Tomko

et al. 2013

Journal of Biological Chemistry

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Background: New regulators of the ubiquitin-proteasome system (UPS) were sought in yeast. Results: Cuz1 (Cdc48-associated ubiquitin-like/zinc finger protein-1) interacts with the Cdc48/p97 ATPase and promotes endoplasmic reticulum-associated degradation. Conclusion: Cuz1 is a highly conserved Cdc48 cofactor that also binds proteasomes, especially in cells exposed to arsenite. Significance: This first characterization of the Cuz1 protein family links it to specific Cdc48/p97 complexes.

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The UBX domain: a widespread ubiquitin-like module

Cited by 135 publications

References 40 publications

Socius Is a Novel Rnd GTPase-Interacting Protein Involved in Disassembly of Actin Stress Fibers

Socius Is a Novel Rnd GTPase-Interacting Protein Involved in Disassembly of Actin Stress Fibers

Control of p97 function by cofactor binding

A Conserved Protein with AN1 Zinc Finger and Ubiquitin-like Domains Modulates Cdc48 (p97) Function in the Ubiquitin-Proteasome Pathway

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