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Systematic substrate identification indicates a central role for the metalloprotease ADAM10 in axon targeting and synapse function

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Systematic substrate identification indicates a central role for the metalloprotease ADAM10 in axon targeting and synapse function. / Kuhn, Peer-Hendrik; Colombo, Alessio Vittorio; Schusser, Benjamin; Dreymueller, Daniela; Wetzel, Sebastian; Schepers, Ute; Herber, Julia; Ludwig, Andreas; Kremmer, Elisabeth; Montag, Dirk; Müller, Ulrike; Schweizer, Michaela; Saftig, Paul; Bräse, Stefan; Lichtenthaler, Stefan F.

in: ELIFE, Jahrgang 5, 23.01.2016, S. e12748.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Kuhn, P-H, Colombo, AV, Schusser, B, Dreymueller, D, Wetzel, S, Schepers, U, Herber, J, Ludwig, A, Kremmer, E, Montag, D, Müller, U, Schweizer, M, Saftig, P, Bräse, S & Lichtenthaler, SF 2016, 'Systematic substrate identification indicates a central role for the metalloprotease ADAM10 in axon targeting and synapse function', ELIFE, Jg. 5, S. e12748.

APA

Kuhn, P-H., Colombo, A. V., Schusser, B., Dreymueller, D., Wetzel, S., Schepers, U., Herber, J., Ludwig, A., Kremmer, E., Montag, D., Müller, U., Schweizer, M., Saftig, P., Bräse, S., & Lichtenthaler, S. F. (2016). Systematic substrate identification indicates a central role for the metalloprotease ADAM10 in axon targeting and synapse function. ELIFE, 5, e12748.

Vancouver

Kuhn P-H, Colombo AV, Schusser B, Dreymueller D, Wetzel S, Schepers U et al. Systematic substrate identification indicates a central role for the metalloprotease ADAM10 in axon targeting and synapse function. ELIFE. 2016 Jan 23;5:e12748.

Bibtex

@article{cae9a733b5e94c058c514e4183d301a8,
title = "Systematic substrate identification indicates a central role for the metalloprotease ADAM10 in axon targeting and synapse function",
abstract = "Metzincin metalloproteases have major roles in intercellular communication by modulating the function of membrane proteins. One of the proteases is the a-disintegrin-and-metalloprotease 10 (ADAM10) which acts as alpha-secretase of the Alzheimer's disease amyloid precursor protein. ADAM10 is also required for neuronal network functions in murine brain, but neuronal ADAM10 substrates are only partly known. With a proteomic analysis of Adam10-deficient neurons we identified 91, mostly novel ADAM10 substrate candidates, making ADAM10 a major protease for membrane proteins in the nervous system. Several novel substrates, including the neuronal cell adhesion protein NrCAM, are involved in brain development. Indeed, we detected mistargeted axons in the olfactory bulb of conditional ADAM10-/- mice, which correlate with reduced cleavage of NrCAM, NCAM and other ADAM10 substrates. In summary, the novel ADAM10 substrates provide a molecular basis for neuronal network dysfunctions in conditional ADAM10-/- mice and demonstrate a fundamental function of ADAM10 in the brain.",
author = "Peer-Hendrik Kuhn and Colombo, {Alessio Vittorio} and Benjamin Schusser and Daniela Dreymueller and Sebastian Wetzel and Ute Schepers and Julia Herber and Andreas Ludwig and Elisabeth Kremmer and Dirk Montag and Ulrike M{\"u}ller and Michaela Schweizer and Paul Saftig and Stefan Br{\"a}se and Lichtenthaler, {Stefan F}",
year = "2016",
month = jan,
day = "23",
language = "English",
volume = "5",
pages = "e12748",
journal = "ELIFE",
issn = "2050-084X",
publisher = "eLife Sciences Publications",

}

RIS

TY - JOUR

T1 - Systematic substrate identification indicates a central role for the metalloprotease ADAM10 in axon targeting and synapse function

AU - Kuhn, Peer-Hendrik

AU - Colombo, Alessio Vittorio

AU - Schusser, Benjamin

AU - Dreymueller, Daniela

AU - Wetzel, Sebastian

AU - Schepers, Ute

AU - Herber, Julia

AU - Ludwig, Andreas

AU - Kremmer, Elisabeth

AU - Montag, Dirk

AU - Müller, Ulrike

AU - Schweizer, Michaela

AU - Saftig, Paul

AU - Bräse, Stefan

AU - Lichtenthaler, Stefan F

PY - 2016/1/23

Y1 - 2016/1/23

N2 - Metzincin metalloproteases have major roles in intercellular communication by modulating the function of membrane proteins. One of the proteases is the a-disintegrin-and-metalloprotease 10 (ADAM10) which acts as alpha-secretase of the Alzheimer's disease amyloid precursor protein. ADAM10 is also required for neuronal network functions in murine brain, but neuronal ADAM10 substrates are only partly known. With a proteomic analysis of Adam10-deficient neurons we identified 91, mostly novel ADAM10 substrate candidates, making ADAM10 a major protease for membrane proteins in the nervous system. Several novel substrates, including the neuronal cell adhesion protein NrCAM, are involved in brain development. Indeed, we detected mistargeted axons in the olfactory bulb of conditional ADAM10-/- mice, which correlate with reduced cleavage of NrCAM, NCAM and other ADAM10 substrates. In summary, the novel ADAM10 substrates provide a molecular basis for neuronal network dysfunctions in conditional ADAM10-/- mice and demonstrate a fundamental function of ADAM10 in the brain.

AB - Metzincin metalloproteases have major roles in intercellular communication by modulating the function of membrane proteins. One of the proteases is the a-disintegrin-and-metalloprotease 10 (ADAM10) which acts as alpha-secretase of the Alzheimer's disease amyloid precursor protein. ADAM10 is also required for neuronal network functions in murine brain, but neuronal ADAM10 substrates are only partly known. With a proteomic analysis of Adam10-deficient neurons we identified 91, mostly novel ADAM10 substrate candidates, making ADAM10 a major protease for membrane proteins in the nervous system. Several novel substrates, including the neuronal cell adhesion protein NrCAM, are involved in brain development. Indeed, we detected mistargeted axons in the olfactory bulb of conditional ADAM10-/- mice, which correlate with reduced cleavage of NrCAM, NCAM and other ADAM10 substrates. In summary, the novel ADAM10 substrates provide a molecular basis for neuronal network dysfunctions in conditional ADAM10-/- mice and demonstrate a fundamental function of ADAM10 in the brain.

M3 - SCORING: Journal article

VL - 5

SP - e12748

JO - ELIFE

JF - ELIFE

SN - 2050-084X

ER -