GroEL-substrate interactions: molding the fold, or folding the mold?

Article Abstract:

GroEL-substrate interactions are discussed in this review article. Of the molecular chaperones ensuring proteins have the right folds, chaperonins are now seen as the magic folding machines in mitochondria and chloroplasts and in the eukaryotic and prokaryotic cytosol, TriC and GroEL/ES, respectively. Until recently, two very interesting aspects of GroEL function have been hard to figure out, that is, the structural details that would add to understanding of how many different substrates bind to the chaperonin and the identity of the in vivo substrates of this very abundant molecule. These are discussed in the light of recent research. Topics include a flexible peptide-binding groove, conformations bound ligands assume, substrates in vivo, and possible mechanisms.

Escherichia coli, Cellular control mechanisms, Cell regulation, Polypeptides, Structure-activity relationships (Biochemistry)

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Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain

Article Abstract:

The structure of the ezrin-radixin-moesin (ERM) protein moesin has been shown to reveal the four-point-one, ezrin, radixin, moesin homology (FERM) domain fold masked by an extended actin-binding tail domain. A novel mechanism through which different signals could bring on varying degrees of activation is suggested. The FERM domain has three compact lobes with an integrated PTB/PH/EVH1 fold. The C-terminal segment is bound as an extended peptide masking a large FERM domain surface. GERM domains are involved in localizing proteins to the plasma membrane

Membrane proteins, Cell membranes, Plasma membranes, Actin

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The osteoclast differentiation factor osteoprotegerin-ligand is essential for mammary gland development

Article Abstract:

The osteoclast differentiation factor osteoprotegerin-ligand (OPGL), essential for bone remodeling, has been found to be required for mammary gland development. Mice that have no OPGL or lack its receptor RANK fail to form lobulo-alveolar mammary structures in pregnancy, resulting in death of newborns. The data give a novel paradigm in mammary gland development and give a rationale related to evolution for hormonal regulation and gender bias for female osteoporosis.

South Korea, Canada, Statistical Data Included, Genetic aspects, Evolution (Biology), Evolution, Cell differentiation, Osteoporosis, Mammary glands, Bone morphogenetic proteins

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