Mitochondria: FKBP38 and mitochondrial degradation

Michiko Shirane-Kitsuji, Keiichi I. Nakayama

Research output: Contribution to journalShort surveypeer-review

23 Citations (Scopus)


FK506-binding protein 38 (FKBP38) is a membrane chaperone that is localized predominantly to mitochondria and contains a COOH-terminal tail anchor. FKBP38 also harbors an FKBP domain that confers peptidyl-prolyl cis-trans isomerase activity, but it differs from other FKBP family members in that this activity is dependent on the binding of Ca2+-calmodulin. FKBP38 inhibits apoptosis by recruiting the anti-apoptotic proteins Bcl-2 and Bcl-xL to mitochondria. Mice deficient in FKBP38 die soon after birth manifesting a defect in neural tube closure that results in part from unrestrained apoptosis. We recently found that FKBP38 and Bcl-2 translocate from mitochondria to the endoplasmic reticulum during mitophagy, a form of autophagy responsible for the elimination of damaged mitochondria. FKBP38 and Bcl-2 thus escape the degradative fate of most mitochondrial proteins during mitophagy. This escape of FKBP38 is dependent on the low basicity of its COOH-terminal sequence and is essential for the suppression of apoptosis during mitophagy. FKBP38 thus plays a key role in the regulation of apoptosis under normal and pathological conditions.

Original languageEnglish
Pages (from-to)19-22
Number of pages4
JournalInternational Journal of Biochemistry and Cell Biology
Issue number1
Publication statusPublished - Jun 2014

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Cell Biology


Dive into the research topics of 'Mitochondria: FKBP38 and mitochondrial degradation'. Together they form a unique fingerprint.

Cite this