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Mitochondrial E3 ubiquitin ligase 1 (Mul1) is a multifunctional mitochondrial membrane protein with its RING domain exposed to the cytoplasm. On the one hand, Mul1 functions as a ubiquitin-ligase to ubiquitinate a bunch of signal molecules, such as mitofusin2 (Mfn2), Akt, p53 and ULK1, through its RING finger domain, leading to proteins degradation. On the other hand, Mul1 acts as a small ubiquitin-like modifiers (SUMO) E3 ligase to sumoylate certain proteins, such as dynamin-related protein 1 (Drp1), enhancing protein stabilization. Through the dual functions of ubiquitination and SUMOylation, Mul1 involves in regulation of many physiological and pathological processes, such as mitochondrial dynamics, cell growth, apoptosis and mitophagy. In addition, Mul1 can also directly activate or interact with some proteins, such as NF-κB and JNK, to take part in the regulation of cellular apoptosis. This review summarizes recent progress in relevant studies on the physiological and pathological functions of Mul1 and pays special attention to its role in regulation of mitochondrial dynamics. [ABSTRACT FROM AUTHOR]