Biochemical and genetic studies of UBR3, a ubiquitin ligase with a function in olfactory and other sensory systems.

Biochemical and genetic studies of UBR3, a ubiquitin ligase with a function in olfactory and other sensory systems. Research Abstract Details 

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Biochemical and genetic studies of UBR3, a ubiquitin ligase with a function in olfactory and other sensory systems. Abstract Text:

Takafumi Tasaki,Reinhard Sohr,Zanxian Xia,Rainer Hellweg,Heide ,Alexander Varshavsky,Yong Tae Kwon,

Our previous work identified E3 ubiquitin ligases, termed UBR1-UBR7, that contain the approximately 70-residue UBR box, a motif important for the targeting of N-end rule substrates. In this pathway, specific N-terminal residues of substrates are recognized as degradation signals by UBR box-containing E3s that include UBR1, UBR2, UBR4, and UBR5. The other E3s of this set, UBR3, UBR6, and UBR7, remained uncharacterized. Here we describe the cloning and analyses of mouse UBR3. The similarities of UBR3 to the UBR1 and UBR2 E3s of the N-end rule pathway include the RING and UBR domains. We show that HR6A and HR6B, the E2 enzymes that bind to UBR1 and UBR2, also interact with UBR3. However, in contrast to UBR1 and UBR2, UBR3 does not recognize N-end rule substrates. We also constructed UBR3-lacking mouse strains. In the 129SvImJ background, UBR3-/- mice died during embryogenesis, whereas the C57BL/6 background UBR3-/- mice exhibited neonatal lethality and suckling impairment that could be partially rescued by litter size reduction. The adult UBR3-/- mice had female-specific behavioral anosmia. Cells of the olfactory pathway were found to express beta-galactosidase (LacZ) that marked the deletion/disruption UBR3- allele. The UBR3-specific LacZ expression was also prominent in cells of the touch, vision, hearing, and taste systems, suggesting a regulatory role of UBR3 in sensory pathways, including olfaction. By analogy with functions of the UBR domain in the N-end rule pathway, we propose that the UBR box of UBR3 may recognize small compounds that modulate the targeting, by this E3, of its currently unknown substrates.

Biochemical and genetic studies of UBR3, a ubiquitin ligase with a function in olfactory and other sensory systems. Publishing Authors By Initials

T Tasaki,R Sohr,Z Xia,R Hellweg,H ,A Varshavsky,YT Kwon,

For similar enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: galactosidases: beta-galactosidase research abstracts see: enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: galactosidases: beta-galactosidase research

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Biochemical and genetic studies of UBR3, a ubiquitin ligase with a function in olfactory and other sensory systems. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 18510-20

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 26

MONTH: 04

YEAR: 2007

Biochemical and genetic studies of UBR3, a ubiquitin ligase with a function in olfactory and other sensory systems. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Biochemical and genetic studies of UBR3, a ubiquitin ligase with a function in olfactory and other sensory systems. Keywords Mesh Terms:

KEYWORDS: beta-Galactosidase

MESH TERMS: metabolism

Chemical & Substance for Abstract: Biochemical and genetic studies of UBR3, a ubiquitin ligase with a function in olfactory and other sensory systems. Information

Substance Name: Ubiquitin-Protein Ligases

Registry Number: EC 6.3.2.19

Grant and Affiliation Information for Biochemical and genetic studies of UBR3, a ubiquitin ligase with a function in olfactory and other sensory systems.

AFFILIATION: Center for Pharmacogenetics and Department of Pharmaceutical Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, USA.

Country: United States

AGENCY: United States NHLBI

GRANT: HL083365

ACRONYM: HL

MEDLINETA: J Biol Chem

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