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Jörg Höhfeld
© Jörg Höhfeld
Prof. Dr. Jörg Höhfeld
TRA Steering Committee

Website

Affiliations
  • Institut für Zellbiologie
Research topics
  • cell stress
  • protein aggregation
  • protein degradation
Proteins exert their functions in our cells and tissues because they adopt a defined three dimensional structure. Stressful conditions, such as increased temperature or oxidative stress, can cause protein unfolding and thus disturb the integrity of the proteome. As a protective measure cells employ molecular chaperones, which recognize unfolded proteins, prevent their aggregation and promote folding to the functional conformation. In case of terminal damage, chaperones cooperate with cellular degradation systems to facilite protein disposal. We are studying molecular mechanisms essential for proteome maintenance and elucidate its regulation in diseases.
Selected publications

Tawo R, Pokrzywa W, Kevei E, Akyuz ME, Balaji V, Adrian S, Höhfeld J*, Hoppe T* (2017) The ubiquitin ligase CHIP integrates proteostasis and aging by regulation of insulin receptor turnover. Cell 169:470-482. *shared senior authorship

Ulbricht A, Gehlert S, Leciejewski B, Schiffer T, Bloch W, Höhfeld J (2015) Induction and adaptation of chaperone-assisted selective autophagy CASA in response to resistance exercise in human skeletal muscle. Autophagy 11:538-546.

Ulbricht A, Eppler FJ, Tapia VE, Van Der Ven PFM, Hampe N, Hersch N, Vakeel P, Stadel D, Haas A, Saftig P, Behrends C, Fürst DO, Volkmer R, Hoffmann B, Kolanus W, Höhfeld J (2013) Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy. Curr Biol 23:430–435.

Arndt V, Dick N, Tawo R, Dreiseidler M, Wenzel D, Hesse M, Fürst DO, Saftig P, Saint R, Fleischmann BK, Hoch M, Höhfeld J (2010) Chaperone-Assisted Selective Autophagy Is Essential for Muscle Maintenance. Curr Biol 20:143–148.

Jörg Höhfeld
© Jörg Höhfeld
Prof. Dr. Jörg Höhfeld
TRA Steering Committee

Website

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