<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Ackema KB</dc:creator>
  <dc:creator>Hench J</dc:creator>
  <dc:creator>Böckler S</dc:creator>
  <dc:creator>Wang SC</dc:creator>
  <dc:creator>Sauder U</dc:creator>
  <dc:creator>Mergentaler H</dc:creator>
  <dc:creator>Westermann B</dc:creator>
  <dc:creator>Bard F</dc:creator>
  <dc:creator>Frank S</dc:creator>
  <dc:creator>Spang A</dc:creator>
  <dc:date>2014</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">The small GTPase Arf1 plays critical roles in membrane traffic by initiating the recruitment of coat proteins and by modulating the activity of lipid-modifying enzymes. Here, we report an unexpected but evolutionarily conserved role for Arf1 and the ArfGEF GBF1 at mitochondria. Loss of function of ARF-1 or GBF-1 impaired mitochondrial morphology and activity in Caenorhabditis elegans. Similarly, mitochondrial defects were observed in mammalian and yeast cells. In Saccharomyces cerevisiae, aberrant clusters of the mitofusin Fzo1 accumulated in arf1-11 mutants and were resolved by overexpression of Cdc48, an AAA-ATPase involved in ER and mitochondria-associated degradation processes. Yeast Arf1 co-fractionated with ER and mitochondrial membranes and interacted genetically with the contact site component Gem1. Furthermore, similar mitochondrial abnormalities resulted from knockdown of either GBF-1 or contact site components in worms, suggesting that the role of Arf1 in mitochondrial functioning is linked to ER-mitochondrial contacts. Thus, Arf1 is involved in mitochondrial homeostasis and dynamics, independent of its role in vesicular traffic.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://sonar.ch/global/documents/201722</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.15252/embj.201489039</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/pmid/25190516</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:source>The EMBO journal. - 2014</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Cdc48</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">ER–mitochondrial contact sites</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">mitochondria‐associated degradation</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">mitophagy</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">stress response</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">ADP-Ribosylation Factor 1</dc:subject>
  <dc:subject xmlns:ns7="xml" ns7:lang="en">Animals</dc:subject>
  <dc:subject xmlns:ns8="xml" ns8:lang="en">Caenorhabditis elegans</dc:subject>
  <dc:subject xmlns:ns9="xml" ns9:lang="en">Caenorhabditis elegans Proteins</dc:subject>
  <dc:subject xmlns:ns10="xml" ns10:lang="en">GTP Phosphohydrolases</dc:subject>
  <dc:subject xmlns:ns11="xml" ns11:lang="en">Membrane Proteins</dc:subject>
  <dc:subject xmlns:ns12="xml" ns12:lang="en">Mitochondria</dc:subject>
  <dc:subject xmlns:ns13="xml" ns13:lang="en">Mitochondrial Membranes</dc:subject>
  <dc:subject xmlns:ns14="xml" ns14:lang="en">Mitochondrial Proteins</dc:subject>
  <dc:subject xmlns:ns15="xml" ns15:lang="en">Saccharomyces cerevisiae</dc:subject>
  <dc:subject xmlns:ns16="xml" ns16:lang="en">Saccharomyces cerevisiae Proteins</dc:subject>
  <dc:title xmlns:ns17="xml" ns17:lang="en">The small GTPase Arf1 modulates mitochondrial morphology and function.</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
