AG Steinberg

Endosomal Dynamics in Health and Disease

Group overview:

My group is funded by an Emmy Noether Junior Research Fellowship of the German Research Council (DFG). We are interested and actively investigate all aspects of endosomal biology with a focus on the endosomal recycling system. Endosomes are highly dynamic vesicular and tubular organelles that transport internalized receptors, adhesion molecules or transporters through the interior of the cells to maintain their distribution across the cellular compartments. Impaired endosomal transport is increasingly recognized as a major contributor to many devastating pathologies such as Alzheimer’s disease or Parkinsonism, which makes it important to understand the function and molecular mechanisms governing the endosomal network.
To investigate how endosomes operate on a molecular level we employ tissue culture of mammalian cells, CRISPR-CAS9 based genome editing, state of the art quantitative proteomics as well as high resolution microscopy techniques. In particular, we use these methods to study proteins that reside on the cytosolic side of endosomes, such as sorting nexins (SNXs), Rab GTPases and an endosomal coat complex called the retromer complex.



Control of RAB7 activity and localization through the retromer/TBC1D5 complex enables RAB7 dependent mitophagy. Jimenez-Orgaz AJ, Kvainickas A, Denner J, Eimer S, Dengjel J, Steinberg F, EMBOJ, 2018 Jan 17


Cargo selective SNX-BAR proteins mediate retromer trimer independent retrograde transport. Kvainickas A, Jimenez-Orgaz AJ, Nägele H, Dengjel J, Steinberg F
J Cell Biol, 2017, Nov 6.

Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling.
McNally KE, Faulkner R, Steinberg F*, Gallon M, Ghai R, Pim D, Langton P, Pearson N, Danson CM, Nägele H, Morris LL, Singla A, Overlee BL, Heesom KJ, Sessions R, Banks L, Collins BM, Berger I, Billadeau DD, Burstein E, Cullen PJ. Nat Cell Biol. 2017 Sep 11
*Co-First and Co-corresponding author

Retromer- and WASH-dependent sorting of nutrient transporters requires a multivalent interaction network with ANKRD50.
Kvainickas A, Jimenez-Orgaz AJ, Nägele H, Diedrich B, Heesom KJ, Dengjel J, Cullen PJ, Steinberg F
J Cell Sci. 2017 Jan 15

A unique PDZ domain and arrestin-like fold interaction reveals mechanistic details of endocytic recycling by SNX27-retromer.
Gallon M, Clairfeuille T, Steinberg F, Mas C, Ghai R, Sessions RB, Teasdale RD, Collins BM, Cullen PJ. Proc Natl Acad Sci U S A. 2014 Sep 2;111(35):E3604-13.

Retromer binding to FAM21 and the WASH complex is perturbed by the Parkinson disease-linked VPS35(D620N) mutation.
McGough IJ, Steinberg F, Jia D, Barbuti PA, McMillan KJ, Heesom KJ, Whone AL, Caldwell MA, Billadeau DD, Rosen MK, Cullen PJ. Curr Biol. 2014 Jul

A global analysis of SNX27-retromer assembly and cargo specificity reveals a role in glucose and metal ion transport
Steinberg F, Gallon M, Winfield MO, Heesom K, Tavare J, Cullen PJ
2013, Nat Cell Biol

SNX17 protects integrins from degradation by sorting between lysosomal and recycling
Steinberg F, Heesom K, Bass MD, Cullen PJ
J Cell Biol. 2012 Apr 16;197(2):219-30

Rapid fusion and syncytium formation of heterologous cells upon expression of the FGFRL1 receptor.
Steinberg F, Gerber SD, Rieckmann T, Trueb B.
J Biol Chem. 2010 Nov 26;285(48):37704-15.

The FGFRL1 receptor is shed from cell membranes, binds fibroblast growth factors (FGFs), and antagonizes FGF signaling in Xenopus embryos.
Steinberg F, Zhuang L, Beyeler M, Kälin RE, Mullis PE, Brändli AW, Trueb B.
J Biol Chem. 2010 Jan 15;285(3):2193-202.




Contact:Dr. Florian Steinberg
Fon:+49 (0)761 203 97198








Center for Biological Systems Analysis

University of Freiburg


  • Address:

    Habsburgerstr. 49
    79104 Freiburg
  • Delivery entrance:

    Hauptstr. 1
    79104 Freiburg


Personal tools