Physiol. Genomics AJP: Endocrinology and Metabolism
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Physiol. Genomics 17: 253-263, 2004; doi:10.1152/physiolgenomics.00226.2003
1094-8341/04 $5.00
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Physiological Genomics 17:253-263 (2004)
1094-8341/04 $5.00 © 2004 American Physiological Society

Invited Review

Parkin and relatives: the RBR family of ubiquitin ligases

Ignacio Marín 1, J. Ignasi Lucas 1, Ana-Citlali Gradilla 2,3 and Alberto Ferrús 2

1 Departamento de Genética, Universidad de Valencia, 46100 Burjassot, Valencia, Spain
2 Instituto Cajal, CSIC, 28002 Madrid, Spain
3 Universidad de Guadalajara, Jalisco, Mexico

Mutations in the parkin gene cause autosomal-recessive juvenile parkinsonism. Parkin encodes a ubiquitin-protein ligase characterized by having the RBR domain, composed of two RING fingers plus an IBR/DRIL domain. The RBR family is defined as the group of genes whose products contain an RBR domain. RBR family members exist in all eukaryotic species for which significant sequence data is available, including animals, plants, fungi, and several protists. The integration of comparative genomics with structural and functional data allows us to conclude that RBR proteins have multiple roles, not only in protein quality control mechanisms, but also as indirect regulators of transcription. A recently formulated hypothesis, based on a case of gene fusion, suggested that RBR proteins may be often part of cullin-containing ubiquitin ligase complexes. Recent data on Parkin protein agrees with that hypothesis. We discuss the involvement of RBR proteins in several neurodegenerative diseases and cancer.

Parkinson disease; protein quality control; transcriptional regulation




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