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Univ. Prof. Dr. Paul Saftig

Paul Saftig
Paul Saftig
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Molecular Cell Biology and Transgenic Research
 
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News - Biochemisches Institut - Paul Saftig

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3 newsitems found. Page 1 of 1.
A pathway to lysosome revealed
Phospholipase D3 (PLD3) is a protein of unclear function, and little is known in regard to its subcellular localization, its intracellular
trafficking, or function as a putative enzyme. Variants in the phospholipase D3 (PLD3) gene have
genetically been linked to late-onset Alzheimer’s
disease.

We investigated the biosynthetic pathway of PLD3 in order to gain insight into its molecular function and provide the basis for investigating a possible contribution of PLD3 to Alzheimer’s disease (AD)-related cellular processes, particularly in the lysosomal degradative pathway.

PLD3 is proteolytically processed to a soluble form that is stable within endosomes and lysosomes. Its mode of transport from the endoplasmic reticulum to post- Golgi compartments involving proteolytic processing is uncommon
for a luminal lysosomal protein in mammalian cells and involves sorting into intraluminal vesicles of multivesicular bodies(MVBs) of endosomes. The intraluminal sorting events involve ubiquitination and depend on the generation of phosphatidylinositol (PtdIns) (3)P and essential components of the endosomal sorting complexes required for transport (ESCRT) pathway.
This is similar to the delivery pathway of carboxypeptidase S in the budding yeast Saccharomyces cerevisiae, which resembles the prototypic example of a biosynthetic cargo that undergoes ubiquitin-mediated sorting.


Gonzalez, AC, Jagdmann, S., Schweizer, M., Bernreuther,C., Reinheckel, T.,
Saftig, P, Damme, M. (2018)
Unconventional trafficking of mammalian phospholipase D3 to lysosomes.
Cell Rep., Jan 23d, 2018

A pathway to lysosome revealed
Phospholipase D3 (PLD3) is a protein of unclear function, and little is known in regard to its subcellular localization, its intracellular
trafficking, or function as a putative enzyme. Variants in the phospholipase D3 (PLD3) gene have
genetically been linked to late-onset Alzheimer’s
disease.

We investigated the biosynthetic pathway of
PLD3 in order to gain insight into its molecular function and provide the basis for investigating a possible contribution of PLD3 to Alzheimer’s disease (AD)-related cellular processes, particularly in the lysosomal degradative pathway. PLD3 is proteolytically processed to a soluble form that is stable within endosomes and lysosomes. Its mode of transport from the endoplasmic reticulum to post- Golgi compartments involving proteolytic processing is uncommon
for a luminal lysosomal protein in mammalian cells and involves sorting into intraluminal vesicles of multivesicular bodies(MVBs) of endosomes. The intraluminal sorting events involve ubiquitination and depend on the generation of phosphatidylinositol (PtdIns) (3)P and essential components of the endosomal sorting complexes required for transport (ESCRT) pathway.
This is similar to the delivery pathway of carboxypeptidase S in the budding yeast Saccharomyces cerevisiae, which resembles the prototypic example of a biosynthetic cargo that undergoes ubiquitin-mediated sorting.


Gonzalez, AC, Jagdmann, S., Schweizer, M., Bernreuther,C., Reinheckel, T.,
Saftig, P, Damme, M. (2018)
Unconventional trafficking of mammalian phospholipase D3 to lysosomes.
Cell Rep., Jan 23d, 2018

Postdoc and PhD wanted
Job announcement

The Biochemical Institute as part of the medical Faculty at the Christian Albrechts- University Kiel (Germany) has openings for

two Postdoctoral Research Scientists

and one Ph.D. Student

in the Department of Molecular Cell Biology and Transgenic Biology (Prof. Dr. P. Saftig) to do research in the field of lysosome biology, neurodegenerative disorders and the development of novel therapeutic strategies.

The positions are available from 4/2018 for a period of 3 years with a possibility for prolongation. The postdoc position with a possible qualification to habilitation or equivalent is paid according to previous experiences (E 13 or 14 TV-L) and the Ph.D. position according to E 13 TV-L. The regular weekly working hours amount to 65 % of a full time position (currently 25,155 hours/Ph.D. position) and 100 % of a full time position (currently 38,7 hours/postdoc position). For the postdoc position a contribution to teaching is expected (4 LVS).

The positions are available to study the role of lysosomal membrane proteins, lysosome positioning, targeting of hydrolases, autophagic pathways, lysosomal transport and lysosomal signaling. Using established and to-be-generated mouse models we focus on the role of lysosomes in the central nervous system and try to understand their contribution in disorders leading to cellular dysfunction and cell death.

Selection of our recent reviews related to our work on lysosomes: Schwake et al. (2013) Traffic 14(7):739-48.; Schröder BA, et al. (2010) Proteomics 10(22):4053-76; Damme M, et al. (2015) Acta Neuropathol 129(3):337-62; Saftig P. and Klumperman J. (2009) Nat Rev Mol Cell Biol 10(9):623-35.

We seek enthusiastic, highly motivated people to join our international research group. The projects involve the analysis of genetic mouse models, cell-based assays, microscopy, molecular biology and histology techniques. Previous experience in these methodologies and a background in molecular biology, cell biology, biochemistry or immunology is provided. Expected are (postdoc positions) among others good publications in international and high-level journals.

The University of Kiel strives to increase the proportion of female researchers in research and teaching and therefore calls upon qualified women to apply. Women are given priority in the case of equivalent qualifications, proficiency and professional performance.

The University of Kiel has an equal opportunities policy for persons with recognized disabilities. Disabled persons with the necessary qualifications will therefore be given priority.

Applications by people with a migration background are particularly welcomed.

Please refrain from submitting application photos. Applicants are requested to send a statement of interest, a full CV incl. certificates as names and addresses of at least two references in a single pdf file (deadline: March 10th, 2018) to:

Prof. Dr. Paul Saftig
Biochemisches Institut
CAU Kiel
Olshausenstr. 40
D-24098 Kiel
Germany
email: psaftig@biochem.uni-kiel.de
phone: ++49-(0)431-8802216
fax: ++49-(0)431-8802238
https://www.uni-kiel.de/Biochemie/saftig

two Postdoctoral Research Scientists and one Ph.D. Student


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A pathway to lysosome revealed
Phospholipase D3 (PLD3) is a protein of unclear...
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A pathway to lysosome revealed
Phospholipase D3 (PLD3) is a protein of unclear...
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Postdoc and PhD wanted
Job announcement The Biochemical Institute as...
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