Protein Degradation

Mayer, R. John; Ciechanover, Aaron; Rechsteiner, Martin

doi:10.1002/352760586x

Cited by 9 publications

References 1 publication

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The Lysine48‐Based Polyubiquitin Chain Proteasomal Signal: Not a Single Child Anymore

2012

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The conjugation of ubiquitin (Ub) to proteins is involved in the regulation of many processes. The modification serves as a recognition element in trans, in which downstream effectors bind to the modified protein and determine its fate and/or function. A polyUb chain that is linked through internal lysine (Lys)‐48 of Ub and anchored to an internal Lys residue of the substrate has become the accepted “canonical” signal for proteasomal targeting and degradation. However, recent studies show that the signal is far more diverse and that chains based on other internal linkages, as well as linear or heterologous chains made of Ub and Ub‐like proteins and even monoUb, are recognized by the proteasome. In addition, chains linked to residues other than internal Lys were described, all challenging the current paradigm.

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The Lysine48‐Based Polyubiquitin Chain Proteasomal Signal: Not a Single Child Anymore

2012

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Ubiquitin Binds to a Short Peptide Segment of Hydrolase UCH‐L3: A Study by FCS, RIfS, ITC and NMR

Roth

Freund²,

Möhrle

et al. 2007

ChemBioChem

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Screening for small peptidic affinity tags for the detection of ubiquitin and ubiquitinated proteins yielded the dodecapeptide amide DPDELRFNAIAL-NH(2) as a specific ubiquitin-interacting ligand. A peptide collection--based on crystal structures with ubiquitin-interacting proteins--was designed and confirmed by sequence comparison of ubiquitin-interacting motifs. Four independent physical detection methods demonstrated that the peptide binds to monomeric ubiquitin with an affinity of about 10 muM and with fast on and off rates. Fluorescence correlation spectroscopy with fluorescent peptides showed specific interaction with ubiquitin. Reflectometric interference spectroscopy with surface-immobilized peptides and isothermal calorimetry measurements confirmed the specific binding of ubiquitin and fast rate constants. (1)H,(15)N heteronuclear NMR localised the interaction site across the beta sheet of ubiquitin. The peptide aligns well with the ubiquitin-interacting motif and represents a lead structure for the rational design of high-affinity tags for targeting ubiquitinated protein in vitro and in vivo.

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Circadian oscillators in eukaryotes

Jolma

Lærum

Lillo

et al. 2010

WIREs Mechanisms of Disease

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The biological clock, present in nearly all eukaryotes, has evolved such that organisms can adapt to our planet's rotation in order to anticipate the coming day or night as well as to anticipate unfavorable seasons. As all modern high-precision chronometers, the biological clock uses oscillation as a timekeeping element. In this review we describe briefly the discovery, historical development, and general properties of circadian oscillators. The issue of temperature compensation is discussed and our present understanding of the underlying genetic and biochemical mechanisms in circadian oscillators are described with special emphasis on Neurospora crassa, mammals and plants.

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Protein Degradation

Cited by 9 publications

References 1 publication

The Lysine48‐Based Polyubiquitin Chain Proteasomal Signal: Not a Single Child Anymore

The Lysine48‐Based Polyubiquitin Chain Proteasomal Signal: Not a Single Child Anymore

Ubiquitin Binds to a Short Peptide Segment of Hydrolase UCH‐L3: A Study by FCS, RIfS, ITC and NMR

Circadian oscillators in eukaryotes

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