Mitochondria: FKBP38 and mitochondrial degradation

Michiko Shirane, Keiichi Nakayama

研究成果: ジャーナルへの寄稿小調査

9 引用 (Scopus)

抄録

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.

元の言語英語
ページ(範囲)19-22
ページ数4
ジャーナルInternational Journal of Biochemistry and Cell Biology
51
発行部数1
DOI
出版物ステータス出版済み - 1 1 2014

Fingerprint

Mitochondrial Degradation
Tacrolimus Binding Proteins
Mitochondria
Proteolysis
Degradation
Apoptosis
Peptidylprolyl Isomerase
Apoptosis Regulatory Proteins
Neural Tube Defects
Mitochondrial Proteins
Autophagy
Calmodulin
Alkalinity
Ports and harbors
Anchors
Endoplasmic Reticulum
Tail

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Cell Biology

これを引用

Mitochondria : FKBP38 and mitochondrial degradation. / Shirane, Michiko; Nakayama, Keiichi.

:: International Journal of Biochemistry and Cell Biology, 巻 51, 番号 1, 01.01.2014, p. 19-22.

研究成果: ジャーナルへの寄稿小調査

@article{c70f1053c6ad40dd91ba51a215186632,
title = "Mitochondria: FKBP38 and mitochondrial degradation",
abstract = "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.",
author = "Michiko Shirane and Keiichi Nakayama",
year = "2014",
month = "1",
day = "1",
doi = "10.1016/j.biocel.2014.03.007",
language = "English",
volume = "51",
pages = "19--22",
journal = "International Journal of Biochemistry and Cell Biology",
issn = "1357-2725",
publisher = "Elsevier Limited",
number = "1",

}

TY - JOUR

T1 - Mitochondria

T2 - FKBP38 and mitochondrial degradation

AU - Shirane, Michiko

AU - Nakayama, Keiichi

PY - 2014/1/1

Y1 - 2014/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84897397124&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84897397124&partnerID=8YFLogxK

U2 - 10.1016/j.biocel.2014.03.007

DO - 10.1016/j.biocel.2014.03.007

M3 - Short survey

C2 - 24657651

AN - SCOPUS:84897397124

VL - 51

SP - 19

EP - 22

JO - International Journal of Biochemistry and Cell Biology

JF - International Journal of Biochemistry and Cell Biology

SN - 1357-2725

IS - 1

ER -