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GnT1IP-L specifically inhibits MGAT1 in the Golgi via its luminal domain

Standard

GnT1IP-L specifically inhibits MGAT1 in the Golgi via its luminal domain. / Huang, Hung-Hsiang; Hassinen, Antti; Sundaram, Subha; Spiess, Andrej-Nikolai; Kellokumpu, Sakari; Stanley, Pamela.

in: ELIFE, Jahrgang 4, 2015, S. e08916.

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

Harvard

Huang, H-H, Hassinen, A, Sundaram, S, Spiess, A-N, Kellokumpu, S & Stanley, P 2015, 'GnT1IP-L specifically inhibits MGAT1 in the Golgi via its luminal domain', ELIFE, Jg. 4, S. e08916. https://doi.org/10.7554/eLife.08916

APA

Huang, H-H., Hassinen, A., Sundaram, S., Spiess, A-N., Kellokumpu, S., & Stanley, P. (2015). GnT1IP-L specifically inhibits MGAT1 in the Golgi via its luminal domain. ELIFE, 4, e08916. https://doi.org/10.7554/eLife.08916

Vancouver

Huang H-H, Hassinen A, Sundaram S, Spiess A-N, Kellokumpu S, Stanley P. GnT1IP-L specifically inhibits MGAT1 in the Golgi via its luminal domain. ELIFE. 2015;4: e08916. https://doi.org/10.7554/eLife.08916

Bibtex

@article{d3ea6bd7a73741028cb260a5c0bd2d72,
title = "GnT1IP-L specifically inhibits MGAT1 in the Golgi via its luminal domain",
abstract = "Mouse GnT1IP-L, and membrane-bound GnT1IP-S (MGAT4D) expressed in cultured cells inhibit MGAT1, the N-acetylglucosaminyltransferase that initiates the synthesis of hybrid and complex N-glycans. However, it is not known where in the secretory pathway GnT1IP-L inhibits MGAT1, nor whether GnT1IP-L inhibits other N-glycan branching N-acetylglucosaminyltransferases of the medial Golgi. We show here that the luminal domain of GnT1IP-L contains its inhibitory activity. Retention of GnT1IP-L in the endoplasmic reticulum (ER) via the N-terminal region of human invariant chain p33, with or without C-terminal KDEL, markedly reduced inhibitory activity. Dynamic fluorescent resonance energy transfer (FRET) and bimolecular fluorescence complementation (BiFC) assays revealed homomeric interactions for GnT1IP-L in the ER, and heteromeric interactions with MGAT1 in the Golgi. GnT1IP-L did not generate a FRET signal with MGAT2, MGAT3, MGAT4B or MGAT5 medial Golgi GlcNAc-tranferases. GnT1IP/Mgat4d transcripts are expressed predominantly in spermatocytes and spermatids in mouse, and are reduced in men with impaired spermatogenesis.",
author = "Hung-Hsiang Huang and Antti Hassinen and Subha Sundaram and Andrej-Nikolai Spiess and Sakari Kellokumpu and Pamela Stanley",
year = "2015",
doi = "10.7554/eLife.08916",
language = "English",
volume = "4",
pages = " e08916",
journal = "ELIFE",
issn = "2050-084X",
publisher = "eLife Sciences Publications",

}

RIS

TY - JOUR

T1 - GnT1IP-L specifically inhibits MGAT1 in the Golgi via its luminal domain

AU - Huang, Hung-Hsiang

AU - Hassinen, Antti

AU - Sundaram, Subha

AU - Spiess, Andrej-Nikolai

AU - Kellokumpu, Sakari

AU - Stanley, Pamela

PY - 2015

Y1 - 2015

N2 - Mouse GnT1IP-L, and membrane-bound GnT1IP-S (MGAT4D) expressed in cultured cells inhibit MGAT1, the N-acetylglucosaminyltransferase that initiates the synthesis of hybrid and complex N-glycans. However, it is not known where in the secretory pathway GnT1IP-L inhibits MGAT1, nor whether GnT1IP-L inhibits other N-glycan branching N-acetylglucosaminyltransferases of the medial Golgi. We show here that the luminal domain of GnT1IP-L contains its inhibitory activity. Retention of GnT1IP-L in the endoplasmic reticulum (ER) via the N-terminal region of human invariant chain p33, with or without C-terminal KDEL, markedly reduced inhibitory activity. Dynamic fluorescent resonance energy transfer (FRET) and bimolecular fluorescence complementation (BiFC) assays revealed homomeric interactions for GnT1IP-L in the ER, and heteromeric interactions with MGAT1 in the Golgi. GnT1IP-L did not generate a FRET signal with MGAT2, MGAT3, MGAT4B or MGAT5 medial Golgi GlcNAc-tranferases. GnT1IP/Mgat4d transcripts are expressed predominantly in spermatocytes and spermatids in mouse, and are reduced in men with impaired spermatogenesis.

AB - Mouse GnT1IP-L, and membrane-bound GnT1IP-S (MGAT4D) expressed in cultured cells inhibit MGAT1, the N-acetylglucosaminyltransferase that initiates the synthesis of hybrid and complex N-glycans. However, it is not known where in the secretory pathway GnT1IP-L inhibits MGAT1, nor whether GnT1IP-L inhibits other N-glycan branching N-acetylglucosaminyltransferases of the medial Golgi. We show here that the luminal domain of GnT1IP-L contains its inhibitory activity. Retention of GnT1IP-L in the endoplasmic reticulum (ER) via the N-terminal region of human invariant chain p33, with or without C-terminal KDEL, markedly reduced inhibitory activity. Dynamic fluorescent resonance energy transfer (FRET) and bimolecular fluorescence complementation (BiFC) assays revealed homomeric interactions for GnT1IP-L in the ER, and heteromeric interactions with MGAT1 in the Golgi. GnT1IP-L did not generate a FRET signal with MGAT2, MGAT3, MGAT4B or MGAT5 medial Golgi GlcNAc-tranferases. GnT1IP/Mgat4d transcripts are expressed predominantly in spermatocytes and spermatids in mouse, and are reduced in men with impaired spermatogenesis.

U2 - 10.7554/eLife.08916

DO - 10.7554/eLife.08916

M3 - SCORING: Journal article

C2 - 26371870

VL - 4

SP - e08916

JO - ELIFE

JF - ELIFE

SN - 2050-084X

ER -