Abstract
Protein degradation occurs through several distinct proteolytic pathways for membrane and cytosolic proteins. There is evidence that these processes are linked and that crosstalk among these major protein degradation pathways occurs. Ubiquilins, a family of ubiquitin-binding proteins, are involved in all protein degradation pathways. This minireview provides an overview of ubiquilin function in protein degradation and contrasts it with sequestosome-1 (p62), a protein that also has been implicated in multiple proteolytic pathways.
Received: 2012-2-11
Accepted: 2012-3-21
Published Online: 2012-06-01
Published in Print: 2012-06-01
©2012 by Walter de Gruyter Berlin Boston
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Articles in the same Issue
- Review
- The critical role of adrenomedullin and its binding protein, AMBP-1, in neuroprotection
- Minireview
- Ubiquilins in the crosstalk among proteolytic pathways
- Protein Structure and Function
- A non-cytotoxic but ribonucleolytically specific ribotoxin variant: implication of tryptophan residues in the cytotoxicity of hirsutellin A
- The composite nature of the interaction between nuclear receptors EcR and DHR38
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- New ketomethylene inhibitor analogues: synthesis and assessment of structural determinants for N-domain selective inhibition of angiotensin-converting enzyme
- Cadherin-related protein 24 induces morphological changes and partial cell polarization by facilitating direct cell-cell interactions
- Molecular Medicine
- Analysis of tissue and salivary nicotinamide N-methyltransferase in oral squamous cell carcinoma: basis for the development of a noninvasive diagnostic test for early-stage disease
- Cell Biology and Signaling
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- Small molecule inhibitors of the c-Jun N-terminal kinase (JNK) possess antiviral activity against highly pathogenic avian and human pandemic influenza A viruses
- Matriptase-2 (TMPRSS6) is directly up-regulated by hypoxia inducible factor-1: identification of a hypoxia-responsive element in the TMPRSS6 promoter region
- Rab1 interacts directly with the β2-adrenergic receptor to regulate receptor anterograde trafficking
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