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Published 27 September 2004. doi:10.1083/jcb.200407046
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 166, Number 7, 1027-1039
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Article

 Endophilin B1 is required for the maintenance of mitochondrial morphology

Mariusz Karbowski, Seon-Yong Jeong, and Richard J. Youle

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892

Address correspondence to R.J. Youle, Bldg. 35, Rm. 917, MSC 3407, 35 Lincoln Dr., Bethesda, MD 20892-1414. Tel.: (301) 496-6628. Fax: (301) 402-0380. email: youler{at}ninds.nih.gov

We report that a fatty acyl transferase, endophilin B1, is required for maintenance of mitochondrial morphology. Down-regulation of this protein or overexpression of endophilin B1 lacking the NH2-terminal lipid-modifying domain causes striking alterations of the mitochondrial distribution and morphology. Dissociation of the outer mitochondrial membrane compartment from that of the matrix, and formation of vesicles and tubules of outer mitochondrial membrane, was also observed in both endophilin B1 knockdown cells and after overexpression of the truncated protein, indicating that endophilin B1 is required for the regulation of the outer mitochondrial membrane dynamics. We also show that endophilin B1 translocates to the mitochondria during the synchronous remodeling of the mitochondrial network that has been described to occur during apoptosis. Double knockdown of endophilin B1 and Drp1 leads to a mitochondrial phenotype identical to that of the Drp1 single knockdown, a result consistent with Drp1 acting upstream of endophilin B1 in the maintenance of morphological dynamics of mitochondria.

Key Words: endocytosis; LPAAT; dynamin; membrane tubulation; scission

Abbreviations used in this paper: AIF, apoptosis-inducing factor; IMM, inter mitochondrial membrane; OMM, outer mitochondrial membrane.


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