TY  - JOUR
A1  - Partho, Halder
A1  - Chen, Yi-chun
A1  - Brauckhoff, Janine
A1  - Hofbauer, Alois
A1  - Dabauvalle, Marie-Christine
A1  - Lewandrowski, Urs
A1  - Winkler, Christiane
A1  - Sickmann, Albert
A1  - Buchner, Erich
T1  - Identification of Eps15 as Antigen Recognized by the Monoclonal Antibodies aa2 and ab52 of the Wuerzburg Hybridoma Library against Drosophila Brain
JF  - PLoS One
N2  - The Wuerzburg Hybridoma Library against the Drosophila brain represents a collection of around 200 monoclonal antibodies that bind to specific structures in the Drosophila brain. Here we describe the immunohistochemical staining patterns, the Western blot signals of one- and two-dimensional electrophoretic separation, and the mass spectrometric characterization of the target protein candidates recognized by the monoclonal antibodies aa2 and ab52 from the library. Analysis of a mutant of a candidate gene identified the Drosophila homolog of the Epidermal growth factor receptor Pathway Substrate clone 15 (Eps15) as the antigen for these two antibodies.
KW  - neuropil
KW  - immunohistochemistry techniques
KW  - gel electrophoresis
KW  - immunoprecipitation
KW  - silver staining
KW  - drosophila melanogaster
KW  - antigen processing and recognition
KW  - hybridomas
Y1  - 2011
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-137957
VL  - 6
IS  - 12
ER  - 
TY  - JOUR
A1  - Dombert, Benjamin
A1  - Sivadasan, Rajeeve
A1  - Simon, Christian M.
A1  - Jablonka, Sibylle
A1  - Sendtner, Michael
T1  - Presynaptic Localization of Smn and hnRNP R in Axon Terminals of Embryonic and Postnatal Mouse Motoneurons
N2  - Spinal muscular atrophy (SMA) is caused by deficiency of the ubiquitously expressed survival motoneuron (SMN) protein. SMN is crucial component of a complex for the assembly of spliceosomal small nuclear ribonucleoprotein (snRNP) particles. Other cellular functions of SMN are less characterized so far. SMA predominantly affects lower motoneurons, but the cellular basis for this relative specificity is still unknown. In contrast to nonneuronal cells where the protein is mainly localized in perinuclear regions and the nucleus, Smn is also present in dendrites, axons and axonal growth cones of isolated motoneurons in vitro. However, this distribution has not been shown in vivo and it is not clear whether Smn and hnRNP R are also present in presynaptic axon terminals of motoneurons in postnatal mice. Smn also associates with components not included in the classical SMN complex like RNA-binding proteins FUS, TDP43, HuD and hnRNP R which are involved in RNA processing, subcellular localization and translation. We show here that Smn and hnRNP R are present in presynaptic compartments at neuromuscular endplates of embryonic and postnatal mice. Smn and hnRNP R are localized in close proximity to each other in axons and axon terminals both in vitro and in vivo. We also provide new evidence for a direct interaction of Smn and hnRNP R in vitro and in vivo, particularly in the cytosol of motoneurons. These data point to functions of SMN beyond snRNP assembly which could be crucial for recruitment and transport of RNA particles into axons and axon terminals, a mechanism which may contribute to SMA pathogenesis.
KW  - axons
KW  - spinal cord
KW  - cytosol
KW  - DAPI staining
KW  - immunoprecipitation
KW  - recombinant proteins
KW  - protein interactions
KW  - thoracic diaphragm
Y1  - 2014
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-113655
ER  -