The “Chaperone Technique”

Lon plays the chaperone

In This Issue In This Issue levels of exogenously expressed PRC1 caused unusual cytoplasmic arrays of microtubules in interphase cells. Overexpressed PRC1 bundles microtubules in interphase cells. Bundle up for cytokinesis ew results from Mollinari et al. (page 1175) reveal that cytokinesis requires microtubule bundles to be formed at the spindle midzone and that the mitotic spindle–associated ...

Unfolding the chaperone story

Protein folding in the cell was originally assumed to be a spontaneous process, based on Anfinsen's discovery that purified proteins can fold on their own after removal from denaturant. Consequently cell biologists showed little interest in the protein folding process. This changed only in the mid and late 1980s, when the chaperone story began to unfold. As a result, we now know that in vivo, p...

Chaperone Function: The Orthodox View

Chaperone discovery.

Molecular chaperones assist de novo protein folding and facilitate the refolding of stress-denatured proteins. The molecular chaperone concept was coined nearly 35 years ago, and since then, tremendous strides have been made in understanding how these factors support protein folding. Here, we focus on how various chaperone proteins were first identified to play roles in protein folding. Example...

A chaperone feels the heat

JCB • VOLUME 167 • NUMBER 2 • 2004 190 A chaperone feels the heat chaperone is supposed to keep its cool when temperatures get hot. But Syed Rizvi, Laura Mancino, Malini Raghavan (University of Michigan, Ann Arbor, MI), and colleagues show that calreticulin—a glycoprotein chaperone—starts to melt in the heat. The resulting structural changes actually improve its chaperone activity and may also ...