Publication

Long Unfolded Linkers Facilitate Membrane Protein Import Through the Nuclear Pore Complex

Meinema, A. C., Laba, J. K., Hapsari, R. A., Otten, R., Mulder, F. A. A., Kralt, A., van den Bogaart, G., Lusk, C. P., Poolman, B. & Veenhoff, L. M., 1-Jul-2011, In : Science. 333, 6038, p. 90-93 4 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Meinema, A. C., Laba, J. K., Hapsari, R. A., Otten, R., Mulder, F. A. A., Kralt, A., ... Veenhoff, L. M. (2011). Long Unfolded Linkers Facilitate Membrane Protein Import Through the Nuclear Pore Complex. Science, 333(6038), 90-93. https://doi.org/10.1126/science.1205741

Author

Meinema, Anne C. ; Laba, Justyna K. ; Hapsari, Rizqiya A. ; Otten, Renee ; Mulder, Frans A. A. ; Kralt, Annemarie ; van den Bogaart, Geert ; Lusk, C. Patrick ; Poolman, Bert ; Veenhoff, Liesbeth M. / Long Unfolded Linkers Facilitate Membrane Protein Import Through the Nuclear Pore Complex. In: Science. 2011 ; Vol. 333, No. 6038. pp. 90-93.

Harvard

Meinema, AC, Laba, JK, Hapsari, RA, Otten, R, Mulder, FAA, Kralt, A, van den Bogaart, G, Lusk, CP, Poolman, B & Veenhoff, LM 2011, 'Long Unfolded Linkers Facilitate Membrane Protein Import Through the Nuclear Pore Complex', Science, vol. 333, no. 6038, pp. 90-93. https://doi.org/10.1126/science.1205741

Standard

Long Unfolded Linkers Facilitate Membrane Protein Import Through the Nuclear Pore Complex. / Meinema, Anne C.; Laba, Justyna K.; Hapsari, Rizqiya A.; Otten, Renee; Mulder, Frans A. A.; Kralt, Annemarie; van den Bogaart, Geert; Lusk, C. Patrick; Poolman, Bert; Veenhoff, Liesbeth M.

In: Science, Vol. 333, No. 6038, 01.07.2011, p. 90-93.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Meinema AC, Laba JK, Hapsari RA, Otten R, Mulder FAA, Kralt A et al. Long Unfolded Linkers Facilitate Membrane Protein Import Through the Nuclear Pore Complex. Science. 2011 Jul 1;333(6038):90-93. https://doi.org/10.1126/science.1205741


BibTeX

@article{53abc12afd4b407584cd9b228ca74b9d,
title = "Long Unfolded Linkers Facilitate Membrane Protein Import Through the Nuclear Pore Complex",
abstract = "Active nuclear import of soluble cargo involves transport factors that shuttle cargo through the nuclear pore complex (NPC) by binding to phenylalanine-glycine (FG) domains. How nuclear membrane proteins cross through the NPC to reach the inner membrane is presently unclear. We found that at least a 120-residue-long intrinsically disordered linker was required for the import of membrane proteins carrying a nuclear localization signal for the transport factor karyopherin-a. We propose an import mechanism for membrane proteins in which an unfolded linker slices through the NPC scaffold to enable binding between the transport factor and the FG domains in the center of the NPC.",
keywords = "INTRACELLULAR TRAFFICKING, ARCHITECTURE, TRANSPORT, DOMAIN",
author = "Meinema, {Anne C.} and Laba, {Justyna K.} and Hapsari, {Rizqiya A.} and Renee Otten and Mulder, {Frans A. A.} and Annemarie Kralt and {van den Bogaart}, Geert and Lusk, {C. Patrick} and Bert Poolman and Veenhoff, {Liesbeth M.}",
year = "2011",
month = "7",
day = "1",
doi = "10.1126/science.1205741",
language = "English",
volume = "333",
pages = "90--93",
journal = "Science",
issn = "0036-8075",
publisher = "AMER ASSOC ADVANCEMENT SCIENCE",
number = "6038",

}

RIS

TY - JOUR

T1 - Long Unfolded Linkers Facilitate Membrane Protein Import Through the Nuclear Pore Complex

AU - Meinema, Anne C.

AU - Laba, Justyna K.

AU - Hapsari, Rizqiya A.

AU - Otten, Renee

AU - Mulder, Frans A. A.

AU - Kralt, Annemarie

AU - van den Bogaart, Geert

AU - Lusk, C. Patrick

AU - Poolman, Bert

AU - Veenhoff, Liesbeth M.

PY - 2011/7/1

Y1 - 2011/7/1

N2 - Active nuclear import of soluble cargo involves transport factors that shuttle cargo through the nuclear pore complex (NPC) by binding to phenylalanine-glycine (FG) domains. How nuclear membrane proteins cross through the NPC to reach the inner membrane is presently unclear. We found that at least a 120-residue-long intrinsically disordered linker was required for the import of membrane proteins carrying a nuclear localization signal for the transport factor karyopherin-a. We propose an import mechanism for membrane proteins in which an unfolded linker slices through the NPC scaffold to enable binding between the transport factor and the FG domains in the center of the NPC.

AB - Active nuclear import of soluble cargo involves transport factors that shuttle cargo through the nuclear pore complex (NPC) by binding to phenylalanine-glycine (FG) domains. How nuclear membrane proteins cross through the NPC to reach the inner membrane is presently unclear. We found that at least a 120-residue-long intrinsically disordered linker was required for the import of membrane proteins carrying a nuclear localization signal for the transport factor karyopherin-a. We propose an import mechanism for membrane proteins in which an unfolded linker slices through the NPC scaffold to enable binding between the transport factor and the FG domains in the center of the NPC.

KW - INTRACELLULAR TRAFFICKING

KW - ARCHITECTURE

KW - TRANSPORT

KW - DOMAIN

U2 - 10.1126/science.1205741

DO - 10.1126/science.1205741

M3 - Article

VL - 333

SP - 90

EP - 93

JO - Science

JF - Science

SN - 0036-8075

IS - 6038

ER -

ID: 5356340