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Most mitochondrial proteins are synthesized in the cytosol and targeted to the mitochondrial
surface in a post-translational manner. The surface of the endoplasmic reticulum (ER) plays an
active role in this targeting reaction. ER-associated chaperones interact with certain mitochondrial
membrane protein precursors and transfer them onto receptor proteins of the mitochondrial surface
in a process termed ER-SURF. ATP-driven proteins in the membranes of mitochondria (Msp1, ATAD1)
and the ER (Spf1, P5A-ATPase) serve as extractors for the removal of mislocalized proteins. If the
re-routing to mitochondria fails, precursors can be degraded by ER or mitochondria-associated degradation
(ERAD or MAD respectively) in a proteasome-mediated reaction. This review summarizes the
current knowledge about the cooperation of the ER and mitochondria in the targeting and quality
control of mitochondrial precursor proteins.