Research ExplorerPublicationsA Fragment of Adhesion Molecule L1 Binds to Nuclear Receptor...

A Fragment of Adhesion Molecule L1 Binds to Nuclear Receptors to Regulate Synaptic Plasticity and Motor Coordination

Standard

A Fragment of Adhesion Molecule L1 Binds to Nuclear Receptors to Regulate Synaptic Plasticity and Motor Coordination. / Kraus, Kristina; Kleene, Ralf; Henis, Melad; Braren, Ingke; Kataria, Hardeep; Sharaf, Ahmed; Loers, Gabriele; Schachner, Melitta; Lutz, David.

In: MOL NEUROBIOL, Vol. 55, No. 9, 09.2018, p. 7164-7178.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Kraus, K, Kleene, R, Henis, M, Braren, I, Kataria, H, Sharaf, A, Loers, G, Schachner, M & Lutz, D 2018, 'A Fragment of Adhesion Molecule L1 Binds to Nuclear Receptors to Regulate Synaptic Plasticity and Motor Coordination', MOL NEUROBIOL, vol. 55, no. 9, pp. 7164-7178. https://doi.org/10.1007/s12035-018-0901-7

APA

Kraus, K., Kleene, R., Henis, M., Braren, I., Kataria, H., Sharaf, A., Loers, G., Schachner, M., & Lutz, D. (2018). A Fragment of Adhesion Molecule L1 Binds to Nuclear Receptors to Regulate Synaptic Plasticity and Motor Coordination. MOL NEUROBIOL, 55(9), 7164-7178. https://doi.org/10.1007/s12035-018-0901-7

Vancouver

Kraus K, Kleene R, Henis M, Braren I, Kataria H, Sharaf A et al. A Fragment of Adhesion Molecule L1 Binds to Nuclear Receptors to Regulate Synaptic Plasticity and Motor Coordination. MOL NEUROBIOL. 2018 Sep;55(9):7164-7178. https://doi.org/10.1007/s12035-018-0901-7

Bibtex

@article{f14bffb18d7a442a8189673f2f72fd29,
title = "A Fragment of Adhesion Molecule L1 Binds to Nuclear Receptors to Regulate Synaptic Plasticity and Motor Coordination",
abstract = "Proteolytic cleavage of the neuronal isoform of the murine cell adhesion molecule L1, triggered by stimulation of the cognate L1-dependent signaling pathways, results in the generation and nuclear import of an L1 fragment that contains the intracellular domain, the transmembrane domain, and part of the extracellular domain. Here, we show that the LXXLL and FXXLF motifs in the extracellular and transmembrane domain of this L1 fragment mediate the interaction with the nuclear estrogen receptors α (ERα) and β (ERβ), peroxisome proliferator-activated receptor γ (PPARγ), and retinoid X receptor β (RXRβ). Mutations of the LXXLL motif in the transmembrane domain and of the FXXLF motif in the extracellular domain disturb the interaction of the L1 fragment with these nuclear receptors and, when introduced by viral transduction into mouse embryos in utero, result in impaired motor coordination, learning and memory, as well as synaptic connectivity in the cerebellum, in adulthood. These impairments are similar to those observed in the L1-deficient mouse. Our findings suggest that the interplay of nuclear L1 and distinct nuclear receptors is associated with synaptic contact formation and plasticity.",
author = "Kristina Kraus and Ralf Kleene and Melad Henis and Ingke Braren and Hardeep Kataria and Ahmed Sharaf and Gabriele Loers and Melitta Schachner and David Lutz",
year = "2018",
month = sep,
doi = "10.1007/s12035-018-0901-7",
language = "English",
volume = "55",
pages = "7164--7178",
journal = "MOL NEUROBIOL",
issn = "0893-7648",
publisher = "Humana Press",
number = "9",

}

RIS

TY - JOUR

T1 - A Fragment of Adhesion Molecule L1 Binds to Nuclear Receptors to Regulate Synaptic Plasticity and Motor Coordination

AU - Kraus, Kristina

AU - Kleene, Ralf

AU - Henis, Melad

AU - Braren, Ingke

AU - Kataria, Hardeep

AU - Sharaf, Ahmed

AU - Loers, Gabriele

AU - Schachner, Melitta

AU - Lutz, David

PY - 2018/9

Y1 - 2018/9

N2 - Proteolytic cleavage of the neuronal isoform of the murine cell adhesion molecule L1, triggered by stimulation of the cognate L1-dependent signaling pathways, results in the generation and nuclear import of an L1 fragment that contains the intracellular domain, the transmembrane domain, and part of the extracellular domain. Here, we show that the LXXLL and FXXLF motifs in the extracellular and transmembrane domain of this L1 fragment mediate the interaction with the nuclear estrogen receptors α (ERα) and β (ERβ), peroxisome proliferator-activated receptor γ (PPARγ), and retinoid X receptor β (RXRβ). Mutations of the LXXLL motif in the transmembrane domain and of the FXXLF motif in the extracellular domain disturb the interaction of the L1 fragment with these nuclear receptors and, when introduced by viral transduction into mouse embryos in utero, result in impaired motor coordination, learning and memory, as well as synaptic connectivity in the cerebellum, in adulthood. These impairments are similar to those observed in the L1-deficient mouse. Our findings suggest that the interplay of nuclear L1 and distinct nuclear receptors is associated with synaptic contact formation and plasticity.

AB - Proteolytic cleavage of the neuronal isoform of the murine cell adhesion molecule L1, triggered by stimulation of the cognate L1-dependent signaling pathways, results in the generation and nuclear import of an L1 fragment that contains the intracellular domain, the transmembrane domain, and part of the extracellular domain. Here, we show that the LXXLL and FXXLF motifs in the extracellular and transmembrane domain of this L1 fragment mediate the interaction with the nuclear estrogen receptors α (ERα) and β (ERβ), peroxisome proliferator-activated receptor γ (PPARγ), and retinoid X receptor β (RXRβ). Mutations of the LXXLL motif in the transmembrane domain and of the FXXLF motif in the extracellular domain disturb the interaction of the L1 fragment with these nuclear receptors and, when introduced by viral transduction into mouse embryos in utero, result in impaired motor coordination, learning and memory, as well as synaptic connectivity in the cerebellum, in adulthood. These impairments are similar to those observed in the L1-deficient mouse. Our findings suggest that the interplay of nuclear L1 and distinct nuclear receptors is associated with synaptic contact formation and plasticity.

U2 - 10.1007/s12035-018-0901-7

DO - 10.1007/s12035-018-0901-7

M3 - SCORING: Journal article

VL - 55

SP - 7164

EP - 7178

JO - MOL NEUROBIOL

JF - MOL NEUROBIOL

SN - 0893-7648

IS - 9

ER -