Molecular chaperones: Plugging the transport gap

Plugging the Gap

Plugging the GAP between cell polarity and cell cycle.

the establishment and maintenance of cell polarity—that is, the asymmetrical partitioning of cellular materials—is fundamental to stem-cell renewal and development. the budding yeast Saccharomyces cerevisiae is a leading model organism for studying cell polarity. yeast cell polarity is intimately connected to the organization of the actin cytoskeleton, which guides secretion towards the budding...

Molecular Chaperones

In most cases proteins fold spontaneously under physiological conditions and do not require any external assistance. This has become evident since the experiments on ribonuclease A conducted by Anfinsen in ‘50s and ‘60s. The list of such “successful” folders has grown since and now includes many two-state proteins catalogued in Folding & Design 3, R81. These proteins fold rapidly and reliably t...

Molecular chaperones in the kidney.

The normal milieu of the kidney includes hypoxia, large osmotic fluxes, and an enormous amount of fluid/solute reabsorption. Renal adaptation to these conditions requires a host of molecular chaperones that stabilize protein conformation, target nascent proteins to their final intracellular destination, and prevent protein aggregation. Under physiologic or pharmacologic stress, inducible molecu...

Molecular chaperones: Avoiding the crowd

The involvement of two types of molecular chaperone in folding newly synthesized proteins can be rationalized in terms of the crowded nature of the intracellular environment. Recent work sheds light on how these chaperones recognise their substrates and protect them from the problems of macromolecular crowding.