Myelin basic protein cleaves cell adhesion molecule l1 and promotes neuritogenesis and cell survival.

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Myelin basic protein cleaves cell adhesion molecule l1 and promotes neuritogenesis and cell survival. / Lutz, David; Loers, Gabriele; Kleene, Ralf; Oezen, Iris; Kataria, Hardeep; Katagihallimath, Nainesh; Braren, Ingke ; Harauz, George; Schachner, Melitta.

In: J BIOL CHEM, Vol. 289, No. 19, 05.2014, p. 13503-13518.

Research output: SCORING: Contribution to journalSCORING: Journal articleResearchpeer-review

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Lutz, D, Loers, G, Kleene, R, Oezen, I, Kataria, H, Katagihallimath, N, Braren, I, Harauz, G & Schachner, M 2014, 'Myelin basic protein cleaves cell adhesion molecule l1 and promotes neuritogenesis and cell survival.', J BIOL CHEM, vol. 289, no. 19, pp. 13503-13518. https://doi.org/10.1074/jbc.M113.530238

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Bibtex

@article{50056e7881ba462daf118b4bb58e2387,
title = "Myelin basic protein cleaves cell adhesion molecule l1 and promotes neuritogenesis and cell survival.",
abstract = "The cell adhesion molecule L1 is a Lewis(x)-carrying glycoprotein that plays important roles in the developing and adult nervous system. Here we show that myelin basic protein (MBP) binds to L1 in a Lewis(x)-dependent manner. Furthermore, we demonstrate that MBP is released by murine cerebellar neurons as a sumoylated dynamin-containing protein upon L1 stimulation and that this MBP cleaves L1 as a serine protease in the L1 extracellular domain at Arg(687) yielding a transmembrane fragment that promotes neurite outgrowth and neuronal survival in cell culture. L1-induced neurite outgrowth and neuronal survival are reduced in MBP-deficient cerebellar neurons and in wild-type cerebellar neurons in the presence of an MBP antibody or L1 peptide containing the MBP cleavage site. Genetic ablation of MBP in shiverer mice and mutagenesis of the proteolytically active site in MBP or of the MBP cleavage site within L1 as well as serine protease inhibitors and an L1 peptide containing the MBP cleavage site abolish generation of the L1 fragment. Our findings provide evidence for novel functions of MBP in the nervous system. ",
author = "David Lutz and Gabriele Loers and Ralf Kleene and Iris Oezen and Hardeep Kataria and Nainesh Katagihallimath and Ingke Braren and George Harauz and Melitta Schachner",
year = "2014",
month = may,
doi = "10.1074/jbc.M113.530238",
language = "English",
volume = "289",
pages = "13503--13518",
journal = "J BIOL CHEM",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "19",

}

RIS

TY - JOUR

T1 - Myelin basic protein cleaves cell adhesion molecule l1 and promotes neuritogenesis and cell survival.

AU - Lutz, David

AU - Loers, Gabriele

AU - Kleene, Ralf

AU - Oezen, Iris

AU - Kataria, Hardeep

AU - Katagihallimath, Nainesh

AU - Braren, Ingke

AU - Harauz, George

AU - Schachner, Melitta

PY - 2014/5

Y1 - 2014/5

N2 - The cell adhesion molecule L1 is a Lewis(x)-carrying glycoprotein that plays important roles in the developing and adult nervous system. Here we show that myelin basic protein (MBP) binds to L1 in a Lewis(x)-dependent manner. Furthermore, we demonstrate that MBP is released by murine cerebellar neurons as a sumoylated dynamin-containing protein upon L1 stimulation and that this MBP cleaves L1 as a serine protease in the L1 extracellular domain at Arg(687) yielding a transmembrane fragment that promotes neurite outgrowth and neuronal survival in cell culture. L1-induced neurite outgrowth and neuronal survival are reduced in MBP-deficient cerebellar neurons and in wild-type cerebellar neurons in the presence of an MBP antibody or L1 peptide containing the MBP cleavage site. Genetic ablation of MBP in shiverer mice and mutagenesis of the proteolytically active site in MBP or of the MBP cleavage site within L1 as well as serine protease inhibitors and an L1 peptide containing the MBP cleavage site abolish generation of the L1 fragment. Our findings provide evidence for novel functions of MBP in the nervous system.

AB - The cell adhesion molecule L1 is a Lewis(x)-carrying glycoprotein that plays important roles in the developing and adult nervous system. Here we show that myelin basic protein (MBP) binds to L1 in a Lewis(x)-dependent manner. Furthermore, we demonstrate that MBP is released by murine cerebellar neurons as a sumoylated dynamin-containing protein upon L1 stimulation and that this MBP cleaves L1 as a serine protease in the L1 extracellular domain at Arg(687) yielding a transmembrane fragment that promotes neurite outgrowth and neuronal survival in cell culture. L1-induced neurite outgrowth and neuronal survival are reduced in MBP-deficient cerebellar neurons and in wild-type cerebellar neurons in the presence of an MBP antibody or L1 peptide containing the MBP cleavage site. Genetic ablation of MBP in shiverer mice and mutagenesis of the proteolytically active site in MBP or of the MBP cleavage site within L1 as well as serine protease inhibitors and an L1 peptide containing the MBP cleavage site abolish generation of the L1 fragment. Our findings provide evidence for novel functions of MBP in the nervous system.

U2 - 10.1074/jbc.M113.530238

DO - 10.1074/jbc.M113.530238

M3 - SCORING: Journal article

VL - 289

SP - 13503

EP - 13518

JO - J BIOL CHEM

JF - J BIOL CHEM

SN - 0021-9258

IS - 19

ER -