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Dr. Johannes Egerer - International Federation on Ageing. Berlin, , DE

Dr. Johannes Egerer Dr. Johannes Egerer

Patient Affairs | German Federation for the Blind and Partially Sighted (DBSV)

Berlin, GERMANY

Dr. Egerer researches diabetes and diabetic retinopathy

Social

Industry Expertise (2)

Health and Wellness Research

Areas of Expertise (8)

Genetics German Social System Knowledge Management Eye Diseases Diabetes Diabetic Retinopathy Cell Biology Accessibility of Medical Products

Education (2)

Ludwig-Maximilians Universität München: Ph.D., Biology 2008

Dissertation mit dem Thema: The Golgin GMAP-210
Angefertigt in der Junior Research Group "Intracellular Transport" bei Dr. Francis A. Barr am Max-Planck-Institut für Biochemie Martinsried bei München.

Universität Bayreuth: Diploma, Biochemistry 2003

Languages (3)

  • German
  • English
  • French

Featured Articles (4)

Die Barometer-Studie Der Diabetologe

H.-P. Hammes, J. Egerer, F. Ziemssen, D. Drossel

2017-08-11

Die Barometer Studie wurde von der „International Federation on Ageing“, Internationalen Diabetes-Förderation und der Internationalen Agentur zur Verhinderung von Erblindung durchgeführt. Primäres Ziel war die Identifikation von Barrieren, die ein Screening für Diabetische Retinopathie erschweren. Dabei standen zwei wesentliche Überlegungen im Vordergrund: 1. diabetische Retinopathie ist vermeidbar und 2. diabetische Retinopathie ist behandelbar und damit die diabetesbedingte Erblindung ein vermeidbares Schicksal. Die Studie wurde weltweit in 41 Ländern durchgeführt und stützte sich auf die Befragung von erwachsenen Menschen mit Typ 1 u. Typ 2 Diabetes und Fachleuten aus den Bereichen der Diabetologie und der Ophthalmologie.

Im Folgenden werden die Ergebnisse der globalen Befragung und der speziell in Deutschland durchgeführten Befragung dargestellt…

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Gerodermia osteodysplastica is caused by mutations in SCYL1BP1, a Rab-6 interacting golgin Nature Genetics

2008

Gerodermia osteodysplastica is an autosomal recessive disorder characterized by wrinkly skin and osteoporosis. Here we demonstrate that gerodermia osteodysplastica is caused by loss-of-function mutations in SCYL1BP1, which is highly expressed in skin and osteoblasts. The protein localizes to the Golgi apparatus and interacts with Rab6, identifying SCYL1BP1 as a golgin. These results associate abnormalities of the secretory pathway with age-related changes in connective tissues.

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Functional dissection of Rab GTPases involved in primary cilium formation The Journal of Cell Biology

2007

Primary cilia are sensory structures involved in morphogen signalling during development, liquid flow in the kidney, mechanosensation, sight, and smell (Badano, J.L., N. Mitsuma, P.L. Beales, and N. Katsanis. 2006. Annu. Rev. Genomics Hum. Genet. 7:125–148; Singla, V., and J.F. Reiter. 2006. Science. 313:629–633.). Mutations that affect primary cilia are responsible for several diseases, including neural tube defects, polycystic kidney disease, retinal degeneration, and cancers (Badano et al., 2006; Singla and Reiter, 2006). Primary cilia formation and function requires tight integration of the microtubule cytoskeleton with membrane trafficking (Singla and Reiter, 2006), and this is poorly understood. We show that the Rab GTPase membrane trafficking regulators Rab8a, -17, and -23, and their cognate GTPase-activating proteins (GAPs), XM_037557, TBC1D7, and EVI5like, are involved in primary cilia formation. However, other human Rabs and GAPs are not. Additionally, Rab8a specifically interacts with cenexin/ODF2, a basal body and microtubule binding protein required for cilium biogenesis (Ishikawa, H., A. Kubo, S. Tsukita, and S. Tsukita. 2005. Nat. Cell Biol. 7:517–524), and is the sole Rab enriched at primary cilia. These findings provide a basis for understanding how specific membrane trafficking pathways cooperate with the microtubule cytoskeleton to give rise to the primary cilia.

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Golgi positioning The Journal of Cell Biology

2005

One of the characteristics of the mammalian Golgi is its position adjacent to the nucleus. This characteristic is maintained through the action of the microtubule (MT) minus end–directed motor dynein and MT-associated proteins (MAPs). Recent findings suggest that GMAP-210, a member of the golgin family of proteins, may help to link Golgi membranes and vesicles with the MT cytoskeleton. However, there are good grounds to doubt that either GMAP-210 or its yeast homologue Rud3p is a MAP. Instead, they appear to function in vesicle trafficking events at the Golgi together with the GTPase ARF1 and a small membrane protein, Erv14. As such, the interesting question of how the Golgi interacts with MTs may well remain open to further investigation.

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