Molecular chaperones, like heat shock proteins (hsp), help fold newly made protein chains and move proteins across cell barriers (Craig, 1993; Agard, 1993). Usually, chaperones detach after proteins fold correctly. But sometimes, they stay attached to well-folded proteins in cells. Proteins like Raf and steroid receptors connect with hsp (Wartmann and Davis, 1994; Pratt and Welsh, 1994). For the steroid receptor to work right, it needs to interact with hsp (Pratt and Welsh, 1994). When kinases like Casein kinase II and eIF-2α interact with hsp, their activities increase (Miyata and Yahara, 1992; Szyszka et al., 1989). This shows chaperones help many cell proteins fold and work correctly.
14-3-3 proteins might also act like chaperones. We’re not sure if they help fold proteins, but they boost enzyme activity when attached. This could be because they make the active form of the enzyme more stable. Alam et al. (1994) found that 14-3-3 proteins stop protein clumping in tests and help proteins enter mitochondria. These are jobs chaperones usually do. So, 14-3-3 and hsp proteins might have similar roles.
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