Teis David, Assistenzprofessor Dr.rer.nat

University / Clinic:
Institute: Division Cell Biology, Biocenter, IMU
Research Area: Molecular Cell Biology

Email: david.teis@i-med.ac.at
Web: www.i-med.ac.at/cellbio/labore/Membrane_Traffic_and_Signaling/David_Teis.html

Research Topic:
We are interested in the molecular mechanism that coordinate cell signaling and membrane traffic, in particular during cell surface remodelling. Cell surface remodelling requires the selective degradation of transmembrane proteins in the lysosome. Defects in this essential degradation pathway contribute to hallmarks of cancer such as loss of cell polarity, defects in cell migration and enhanced proliferation and hence can be considered a tumor supressor pathway. постельное белье киев купить

A key step of receptor downregulation occurs on endosomes, where the endosomal complexes required for transport (ESCRTs) sort ubiquitinated cell surface receptors via the multivesicular body (MVB) pathway to the lumen of lysosomes for degradation. This essential, ESCRT-dependent, degradation pathway controls the repertoire of cell surface receptors.Consequently, the ESCRT machinery is involved in diverse developmental processes and its dysfunction contributes to many diseases including cancer and neuro-degeneration. Moreover, the same ESCRT machinery is hijacked by viruses such as HIV to promote their release from host cells. Due to the universal function of the ESCRT machinery in eukaryotes, we use yeast and a combination of biochemistry and imaging as the best suited model system to address the following questions:

1. How does the ESCRT machinery form MVB vesicles ?
2. How do cells react to the loss of ESCRT function? постельное белье купить киев

  The molecular mechanism of ESCRT mediated membrane remodeling
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The regulation of cell growth and survival by selective membrane protein degradation
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Selected publications:
  Alonso Y Adell M, Migliano S, Teis D
ESCRT-III and Vps4: a dynamic multipurpose tool for membrane budding and scission
FEBS J. 2016 Sep;283(18):3288-302. doi: 10.1111/febs.13688. Review.

  Curwin A, Brouwers N, Alonso Y Adell M, Teis D, Turacchio G, Parashuraman S, Ronchi P, Malhotra V
ESCRT-III drives the final stages of CUPS maturation for unconventional protein secretion
Elife. 2016 Apr 26;5. pii: e16299. doi: 10.7554/eLife.16299.

  Müller M, Schmidt O, Angelova M, Faserl K, Weys S, Kremser L, Pfaffenwimmer T, Dalik T, Kraft C, Trajanoski Z, Lindner H, Teis D
The coordinated action of the MVB pathway and autophagy ensures cell survival during starvation.
Elife. 2015 Apr 22;4:e07736.

  Vogel G, Ebner H, de Araujo M, Schmiedinger T, Eiter O, Pircher H, Gutleben K, Witting B, Teis D, Huber L, Hess M
Ultrastructural Morphometry Points to a New Role for LAMTOR2 in Regulating the Endo/Lysosomal System
Traffic. 2015 Jun;16(6):617-34. doi: 10.1111/tra.12271.

  Alonso Y Adell M, Vogel G, Pakdel M, Müller M, Lindner H, Hess M, Teis D
Coordinated binding of Vps4 to ESCRT-III drives membrane neck constriction during MVB vesicle formation. Highlighted in: Nature Cell Biology;
J Cell Biol. 2014 Apr 14;205(1):33-49

  Schiefermeier N, Scheffler J, de Araújo M, Stasyk T, Yordanov T, Ebner H, Offterdinger M, Munck S, Hess M, Wickström S, Lange A, Wunderlich W, Fässler R, Teis D, Huber L
The late endosomal p14-MP1 (LAMTOR2/3) complex regulates focal adhesion dynamics during cell migration.
J Cell Biol. 2014 May 26;205(4):525-40.

  Müller M, Alonso Y Adell M, Teis D
Membrane abscission: first glimpse at dynamic ESCRTs.
Curr Biol. 2012 Aug 7;22(15):R603-5.

  Alonso Y Adell M, Teis D
Assembly and disassembly of the ESCRT-III membrane scission complex
FEBS Lett. 2011 Oct 20;585(20):3191-6

  Morandell S, Grosstessner-Hain K, Roitinger E, Hudecz O, Lindhorst T, Teis D, Wrulich O, Mazanek M, Taus T, Ueberall F, Mechtler K, Huber L
QIKS--Quantitative identification of kinase substrates.
Proteomics. 2010 May;10(10):2015-25.PMID: 20217869

  Teis D, Saksena S, Emr S
SnapShot: the ESCRT machinery.

  Saksena S, Wahlman J, Teis D, Johnson A, Emr S
Functional reconstitution of ESCRT-III assembly and disassembly.

  Teis D, Saksena S, Emr S
Ordered assembly of the ESCRT-III complex on endosomes is required to sequester cargo during MVB formation.
Dev Cell

  Botelho R, Efe J, Teis D, Emr S
Assembly of a Fab1 phosphoinositide kinase signaling complex requires the Fig4 phosphoinositide phosphatase.
Mol Biol Cell

  Teis D, Kurzbauer R, Hilber D, Erlacher M, Villunger A, Geley S, Bohn G, Klein C, Hess M, Huber L
The p14/MP1-scaffold complex is required for endosomal ERK activation and cell cycle progression in vivo.
J Cell Biol. 2006 Dec 18;175(6):861-8.

  Teis D, Taub N, Kurzbauer R, Hilber D, de Araujo M, Erlacher M, Offterdinger M, Villunger A, Geley S, Bohn G, Klein C, Hess M, Huber L
p14-MP1-MEK1 signaling regulates endosomal traffic and cellular proliferation during tissue homeostasis.
J Cell Biol. 2006 Dec 18;175(6):861-

  Teis D, et al.
p14/MP1-NEK1 signaling regulates endosomal traffic and cellular prolioferation during tissue homeostasis.

  Feuerstein I, Morandell S, Stecher G, Huck C, Stasyk T, Huang H, Teis D, Huber L, Bonn G
Phosphoproteomic analysis using immobilized metal ion affinity chromatography on the basis of cellulose powder
Proteomics 2005, 5, 46–54

  Teis D, Kurzbauer R, Hilber D, Erlacher M, Villunger A, Geley S, Bohn G, Klein C, Hess M, Huber L
The p14/MP1-scaffold complex is required for endosomal ERK activation and cell cycle progression in vivo

  Kurzbauer R, Teis D, de Araujo M, Maurer-Stroh S, Eisenhaber F, Bourenkov G, Bartunik H, Hekman M
Crystal structure of the p14

  Kurzbauer R, Teis D, de Araujo M, Maurer-Stroh S, Eisenhaber F, Bourenkov G, Bartunik H, Hekman M, Rapp U, Huber L, Clausen T
Crystal structure of the p14/MP1 scaffolding complex: how a twin couple attaches mitogen-activated protein kinase signaling to late endosomes.
Proc Natl Acad Sci U S A. 2004 Jul 27;101(30):10984-9.

  Teis D, Wunderlich W, Huber L
p14: Localization of the MP1 - MAPK scaffold complex to endosomes is mediated by p14 and required for signal transduction
Dev. Cell 6: 803-14.

  Wunderlich W, Fialka I, Alpi A, Teis D, Pfeifer A, Parton R, Lottspeich F, Huber L
A novel 14 kD protein interacts with the MAP kinase scaffold MP1 on a late endosomal/lysosomal compartment.
J. Cell Biol. 152: 765-776