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Endoplasmic reticulum (ER)-specific chaperones and folding enzymes facilitate folding and unfolding reactions of the newly synthesized proteins in the ER and are known to serve a quality control function, allowing only correctly assembled and folded proteins to exit the compartment. A new study investigates the extent to which proteins leaving the ER return to its folding environment from the Golgi complex. It is concluded that recycling is not induced by misfolded proteins and is not signal-mediated, but could be an inherent property of proteins within the Golgi membranes.

Describes the functions of the membrane protein kinesin as the motor for microtubule-mediated Golgi apparatus-to-endoplasmic reticulum (ER) traffic. Dependence of distribution and dynamics of both ER and Golgi complex on microtubules; Kinesin as the motor powering peripherally directed movements of membrane within the system; Structure-activity relationship of kinesin.