CDKN1B/p27 is localized in mitochondria and improves respiration-dependent processes in the cardiovascular system-New mode of action for caffeine.

We show that the cyclin-dependent kinase inhibitor 1B (CDKN1B)/p27, previously known as a cell cycle inhibitor, is also localized within mitochondria. The migratory capacity of endothelial cells, which need intact mitochondria, is completely dependent on mitochondrial p27. Mitochondrial p27 improves...

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Main Authors: Niloofar Ale-Agha, Christine Goy, Philipp Jakobs, Ioakim Spyridopoulos, Stefanie Gonnissen, Nadine Dyballa-Rukes, Karin Aufenvenne, Florian von Ameln, Mark Zurek, Tim Spannbrucker, Olaf Eckermann, Sascha Jakob, Simone Gorressen, Marcel Abrams, Maria Grandoch, Jens W Fischer, Karl Köhrer, René Deenen, Klaus Unfried, Joachim Altschmied, Judith Haendeler
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2018-06-01
Series:PLoS Biology
Online Access:https://journals.plos.org/plosbiology/article/file?id=10.1371/journal.pbio.2004408&type=printable
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author Niloofar Ale-Agha
Christine Goy
Philipp Jakobs
Ioakim Spyridopoulos
Stefanie Gonnissen
Nadine Dyballa-Rukes
Karin Aufenvenne
Florian von Ameln
Mark Zurek
Tim Spannbrucker
Olaf Eckermann
Sascha Jakob
Simone Gorressen
Marcel Abrams
Maria Grandoch
Jens W Fischer
Karl Köhrer
René Deenen
Klaus Unfried
Joachim Altschmied
Judith Haendeler
author_facet Niloofar Ale-Agha
Christine Goy
Philipp Jakobs
Ioakim Spyridopoulos
Stefanie Gonnissen
Nadine Dyballa-Rukes
Karin Aufenvenne
Florian von Ameln
Mark Zurek
Tim Spannbrucker
Olaf Eckermann
Sascha Jakob
Simone Gorressen
Marcel Abrams
Maria Grandoch
Jens W Fischer
Karl Köhrer
René Deenen
Klaus Unfried
Joachim Altschmied
Judith Haendeler
author_sort Niloofar Ale-Agha
collection DOAJ
description We show that the cyclin-dependent kinase inhibitor 1B (CDKN1B)/p27, previously known as a cell cycle inhibitor, is also localized within mitochondria. The migratory capacity of endothelial cells, which need intact mitochondria, is completely dependent on mitochondrial p27. Mitochondrial p27 improves mitochondrial membrane potential, increases adenosine triphosphate (ATP) content, and is required for the promigratory effect of caffeine. Domain mapping of p27 revealed that the N-terminus and C-terminus are required for those improvements. Further analysis of those regions revealed that the translocation of p27 into the mitochondria and its promigratory activity depend on serine 10 and threonine 187. In addition, mitochondrial p27 protects cardiomyocytes against apoptosis. Moreover, mitochondrial p27 is necessary and sufficient for cardiac myofibroblast differentiation. In addition, p27 deficiency and aging decrease respiration in heart mitochondria. Caffeine does not increase respiration in p27-deficient animals, whereas aged mice display improvement after 10 days of caffeine in drinking water. Moreover, caffeine induces transcriptome changes in a p27-dependent manner, affecting mostly genes relevant for mitochondrial processes. Caffeine also reduces infarct size after myocardial infarction in prediabetic mice and increases mitochondrial p27. Our data characterize mitochondrial p27 as a common denominator that improves mitochondria-dependent processes and define an increase in mitochondrial p27 as a new mode of action of caffeine.
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spelling doaj-art-b537d1dd586d462a80e9c8203d121f2e2025-08-20T02:03:47ZengPublic Library of Science (PLoS)PLoS Biology1544-91731545-78852018-06-01166e200440810.1371/journal.pbio.2004408CDKN1B/p27 is localized in mitochondria and improves respiration-dependent processes in the cardiovascular system-New mode of action for caffeine.Niloofar Ale-AghaChristine GoyPhilipp JakobsIoakim SpyridopoulosStefanie GonnissenNadine Dyballa-RukesKarin AufenvenneFlorian von AmelnMark ZurekTim SpannbruckerOlaf EckermannSascha JakobSimone GorressenMarcel AbramsMaria GrandochJens W FischerKarl KöhrerRené DeenenKlaus UnfriedJoachim AltschmiedJudith HaendelerWe show that the cyclin-dependent kinase inhibitor 1B (CDKN1B)/p27, previously known as a cell cycle inhibitor, is also localized within mitochondria. The migratory capacity of endothelial cells, which need intact mitochondria, is completely dependent on mitochondrial p27. Mitochondrial p27 improves mitochondrial membrane potential, increases adenosine triphosphate (ATP) content, and is required for the promigratory effect of caffeine. Domain mapping of p27 revealed that the N-terminus and C-terminus are required for those improvements. Further analysis of those regions revealed that the translocation of p27 into the mitochondria and its promigratory activity depend on serine 10 and threonine 187. In addition, mitochondrial p27 protects cardiomyocytes against apoptosis. Moreover, mitochondrial p27 is necessary and sufficient for cardiac myofibroblast differentiation. In addition, p27 deficiency and aging decrease respiration in heart mitochondria. Caffeine does not increase respiration in p27-deficient animals, whereas aged mice display improvement after 10 days of caffeine in drinking water. Moreover, caffeine induces transcriptome changes in a p27-dependent manner, affecting mostly genes relevant for mitochondrial processes. Caffeine also reduces infarct size after myocardial infarction in prediabetic mice and increases mitochondrial p27. Our data characterize mitochondrial p27 as a common denominator that improves mitochondria-dependent processes and define an increase in mitochondrial p27 as a new mode of action of caffeine.https://journals.plos.org/plosbiology/article/file?id=10.1371/journal.pbio.2004408&type=printable
spellingShingle Niloofar Ale-Agha
Christine Goy
Philipp Jakobs
Ioakim Spyridopoulos
Stefanie Gonnissen
Nadine Dyballa-Rukes
Karin Aufenvenne
Florian von Ameln
Mark Zurek
Tim Spannbrucker
Olaf Eckermann
Sascha Jakob
Simone Gorressen
Marcel Abrams
Maria Grandoch
Jens W Fischer
Karl Köhrer
René Deenen
Klaus Unfried
Joachim Altschmied
Judith Haendeler
CDKN1B/p27 is localized in mitochondria and improves respiration-dependent processes in the cardiovascular system-New mode of action for caffeine.
PLoS Biology
title CDKN1B/p27 is localized in mitochondria and improves respiration-dependent processes in the cardiovascular system-New mode of action for caffeine.
title_full CDKN1B/p27 is localized in mitochondria and improves respiration-dependent processes in the cardiovascular system-New mode of action for caffeine.
title_fullStr CDKN1B/p27 is localized in mitochondria and improves respiration-dependent processes in the cardiovascular system-New mode of action for caffeine.
title_full_unstemmed CDKN1B/p27 is localized in mitochondria and improves respiration-dependent processes in the cardiovascular system-New mode of action for caffeine.
title_short CDKN1B/p27 is localized in mitochondria and improves respiration-dependent processes in the cardiovascular system-New mode of action for caffeine.
title_sort cdkn1b p27 is localized in mitochondria and improves respiration dependent processes in the cardiovascular system new mode of action for caffeine
url https://journals.plos.org/plosbiology/article/file?id=10.1371/journal.pbio.2004408&type=printable
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