A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphase.
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Summary
A novel SmT3-specific isopeptidase, SMT3IP1, was cloned using a yeast two-hybrid screen with Smt3b as bait and was localized almost exclusively at the nucleolus during interphase.
- Type
- article
- Published
- 2000-11-01
- Cited by
- 179
- References
- 35
- Access
- Open access
- OpenAlex
- https://openalex.org/W1619212443
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:43082151
Keywords
Nucleolus, Interphase, Cell biology, Biology, Nucleus
References
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- PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia.
- Cfi1 prevents premature exit from mitosis by anchoring Cdc14 phosphatase in the nucleolus
- A new protease required for cell-cycle progression in yeast
- Conjugation with the ubiquitin‐related modifier SUMO‐1 regulates the partitioning of PML within the nucleus
- The ubiquitin‐like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer
- SUMO‐1 modification activates the transcriptional response of p53
- A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2.
- Characterization of the cDNA encoding human nucleophosmin and studies of its role in normal and abnormal growth.
- Differential Regulation of Sentrinized Proteins by a Novel Sentrin-specific Protease*
- Mutations in human ARF exon 2 disrupt its nucleolar localization and impair its ability to block nuclear export of MDM2 and p53.
- Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C.
- A New 30-kDa Ubiquitin-related SUMO-1 Hydrolase from Bovine Brain*
- Molecular cloning and characterization of human AOS1 and UBA2, components of the sentrin‐activating enzyme complex
- Ubc9p and the conjugation of SUMO-1 to RanGAP1 and RanBP2.
- Exit from mitosis is triggered by Tem1-dependent release of the protein phosphatase Cdc14 from nucleolar RENT complex.
- The ubiquitin-like proteins SMT3 and SUMO-1 are conjugated by the UBC9 E2 enzyme.
- Identification of Three Major Sentrinization Sites in PML*
- Association of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
Cited by
- In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies.
- Ubiquitin-like protein modifications in prostate and breast cancer.
- Liver receptor homolog‐1 localization in the nuclear body is regulated by sumoylation and cAMP signaling in rat granulosa cells
- Hypocretin-1 and GABA in the Pontine Reticular Formation Interact to Promote Wakefulness.
- Role of ubiquitin-like proteins in transcriptional regulation.
- Expanding PML's functional repertoire through post-translational mechanisms.
- La protéine ING2 : nouvelles fonctions suppressives de tumeurs et régulation par sumoylation
- A NOVEL CARDIAC FUNCTION OF SUMO2/3 AND SENP5 DEPENDENT PATHWAY AND ITS PHYSIOLOGICAL IMPACT ON CONGESTIVE CARDIOMYOPATHY
- The in vivo functions of desumoylating enzymes.
- Molecular mechanisms of oncogénesis mediated by the BTB transcription factor Pipsqueak. Impact of sumoylation and proteolytic processing
- SUMOylation modulates α-synuclein toxicity and fibril formation
- UNDERSTANDING THE ROLE OF SUMOYLATION IN REGULATING LKB1 FUNCTION
- The chromosomal passenger complex during mitotic progression
- Targeting SUMO conjugates for degradation: The human RING finger RNF4 as a specialized ubiquitin ligase
- The SUMO system controls nucleolar partitioning of a novel mammalian ribosome biogenesis complex
- Modificação pós-traducional dependente de SUMO em Schistosoma mansoni : padrão de expressão diferencial durante a transição cercária a esquistossômulo.
- Small ubiquitin-like modifiers in cellular malignancy and metastasis.
- Regulation of FOXO stability and activity by MDM2 E3 ligase
- Evaluation of the activity and substrate specificity of the human SENP family of SUMO proteases.
- Fatty acid acylation regulates trafficking of the unusual P. falciparum calpain to the nucleolus
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