Publication

MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains

Bijlard, M., de Jonge, J. C., Klunder, B., Nomden, A., Hoekstra, D. & Baron, W., 12-May-2016, In : PLoS ONE. 11, 5, 22 p., e0155317.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Bijlard, M., de Jonge, J. C., Klunder, B., Nomden, A., Hoekstra, D., & Baron, W. (2016). MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains. PLoS ONE, 11(5), [e0155317]. https://doi.org/10.1371/journal.pone.0155317

Author

Bijlard, Marjolein ; de Jonge, Jenny C. ; Klunder, Bert ; Nomden, Anita ; Hoekstra, Dick ; Baron, Wia. / MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains. In: PLoS ONE. 2016 ; Vol. 11, No. 5.

Harvard

Bijlard, M, de Jonge, JC, Klunder, B, Nomden, A, Hoekstra, D & Baron, W 2016, 'MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains', PLoS ONE, vol. 11, no. 5, e0155317. https://doi.org/10.1371/journal.pone.0155317

Standard

MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains. / Bijlard, Marjolein; de Jonge, Jenny C.; Klunder, Bert; Nomden, Anita; Hoekstra, Dick; Baron, Wia.

In: PLoS ONE, Vol. 11, No. 5, e0155317, 12.05.2016.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Bijlard M, de Jonge JC, Klunder B, Nomden A, Hoekstra D, Baron W. MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains. PLoS ONE. 2016 May 12;11(5). e0155317. https://doi.org/10.1371/journal.pone.0155317


BibTeX

@article{21aed66047de484a9ca222b0bf4de85e,
title = "MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains",
abstract = "In oligodendrocytes (OLGs), an indirect, transcytotic pathway is mediating transport of de novo synthesized PLP, a major myelin specific protein, from the apical-like plasma membrane to the specialized basolateral-like myelin membrane to prevent its premature compaction. MAL is a well-known regulator of polarized trafficking in epithelial cells, and given its presence in OLGs it was therefore of interest to investigate whether MAL played a similar role in PLP transport in OLGs, taking into account its timely expression in these cells. Our data revealed that premature expression of mCherry-MAL in oligodendrocyte progenitor cells interfered with terminal OLG differentiation, although myelin membrane formation per se was not impaired. In fact, also PLP transport to myelin membranes via the cell body plasma membrane was unaffected. However, the typical shift of PLP from TX-100-insoluble membrane domains to CHAPS-resistant, but TX-100-soluble membrane domains, seen in the absence of MAL expression, is substantially reduced upon expression of the MAL protein. Interestingly, not only in vitro, but also in developing brain a strongly diminished shift from TX-100 resistant to TX-100 soluble domains was observed. Consistently, the MAL-expression mediated annihilation of the typical membrane microdomain shift of PLP is also reflected by a loss of the characteristic surface expression profile of conformation-sensitive anti-PLP antibodies. Hence, these findings suggest that MAL is not involved in vesicular PLP trafficking to either the plasma membrane and/or the myelin membrane as such. Rather, we propose that MAL may regulate PLP's distribution into distinct membrane micro-domains that allow for lateral diffusion of PLP, directly from the plasma membrane to the myelin membrane once the myelin sheath has been assembled.",
keywords = "CENTRAL-NERVOUS-SYSTEM, RAFT-ASSOCIATED PROTEIN, PELIZAEUS-MERZBACHER-DISEASE, PROTEOLIPID PROTEIN, BASIC-PROTEIN, CELL-SURFACE, MONOCLONAL-ANTIBODY, APICAL TRANSPORT, PLASMA-MEMBRANE, RNA TRANSPORT",
author = "Marjolein Bijlard and {de Jonge}, {Jenny C.} and Bert Klunder and Anita Nomden and Dick Hoekstra and Wia Baron",
year = "2016",
month = "5",
day = "12",
doi = "10.1371/journal.pone.0155317",
language = "English",
volume = "11",
journal = "PLOS-One",
issn = "1932-6203",
publisher = "PUBLIC LIBRARY SCIENCE",
number = "5",

}

RIS

TY - JOUR

T1 - MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains

AU - Bijlard, Marjolein

AU - de Jonge, Jenny C.

AU - Klunder, Bert

AU - Nomden, Anita

AU - Hoekstra, Dick

AU - Baron, Wia

PY - 2016/5/12

Y1 - 2016/5/12

N2 - In oligodendrocytes (OLGs), an indirect, transcytotic pathway is mediating transport of de novo synthesized PLP, a major myelin specific protein, from the apical-like plasma membrane to the specialized basolateral-like myelin membrane to prevent its premature compaction. MAL is a well-known regulator of polarized trafficking in epithelial cells, and given its presence in OLGs it was therefore of interest to investigate whether MAL played a similar role in PLP transport in OLGs, taking into account its timely expression in these cells. Our data revealed that premature expression of mCherry-MAL in oligodendrocyte progenitor cells interfered with terminal OLG differentiation, although myelin membrane formation per se was not impaired. In fact, also PLP transport to myelin membranes via the cell body plasma membrane was unaffected. However, the typical shift of PLP from TX-100-insoluble membrane domains to CHAPS-resistant, but TX-100-soluble membrane domains, seen in the absence of MAL expression, is substantially reduced upon expression of the MAL protein. Interestingly, not only in vitro, but also in developing brain a strongly diminished shift from TX-100 resistant to TX-100 soluble domains was observed. Consistently, the MAL-expression mediated annihilation of the typical membrane microdomain shift of PLP is also reflected by a loss of the characteristic surface expression profile of conformation-sensitive anti-PLP antibodies. Hence, these findings suggest that MAL is not involved in vesicular PLP trafficking to either the plasma membrane and/or the myelin membrane as such. Rather, we propose that MAL may regulate PLP's distribution into distinct membrane micro-domains that allow for lateral diffusion of PLP, directly from the plasma membrane to the myelin membrane once the myelin sheath has been assembled.

AB - In oligodendrocytes (OLGs), an indirect, transcytotic pathway is mediating transport of de novo synthesized PLP, a major myelin specific protein, from the apical-like plasma membrane to the specialized basolateral-like myelin membrane to prevent its premature compaction. MAL is a well-known regulator of polarized trafficking in epithelial cells, and given its presence in OLGs it was therefore of interest to investigate whether MAL played a similar role in PLP transport in OLGs, taking into account its timely expression in these cells. Our data revealed that premature expression of mCherry-MAL in oligodendrocyte progenitor cells interfered with terminal OLG differentiation, although myelin membrane formation per se was not impaired. In fact, also PLP transport to myelin membranes via the cell body plasma membrane was unaffected. However, the typical shift of PLP from TX-100-insoluble membrane domains to CHAPS-resistant, but TX-100-soluble membrane domains, seen in the absence of MAL expression, is substantially reduced upon expression of the MAL protein. Interestingly, not only in vitro, but also in developing brain a strongly diminished shift from TX-100 resistant to TX-100 soluble domains was observed. Consistently, the MAL-expression mediated annihilation of the typical membrane microdomain shift of PLP is also reflected by a loss of the characteristic surface expression profile of conformation-sensitive anti-PLP antibodies. Hence, these findings suggest that MAL is not involved in vesicular PLP trafficking to either the plasma membrane and/or the myelin membrane as such. Rather, we propose that MAL may regulate PLP's distribution into distinct membrane micro-domains that allow for lateral diffusion of PLP, directly from the plasma membrane to the myelin membrane once the myelin sheath has been assembled.

KW - CENTRAL-NERVOUS-SYSTEM

KW - RAFT-ASSOCIATED PROTEIN

KW - PELIZAEUS-MERZBACHER-DISEASE

KW - PROTEOLIPID PROTEIN

KW - BASIC-PROTEIN

KW - CELL-SURFACE

KW - MONOCLONAL-ANTIBODY

KW - APICAL TRANSPORT

KW - PLASMA-MEMBRANE

KW - RNA TRANSPORT

U2 - 10.1371/journal.pone.0155317

DO - 10.1371/journal.pone.0155317

M3 - Article

VL - 11

JO - PLOS-One

JF - PLOS-One

SN - 1932-6203

IS - 5

M1 - e0155317

ER -

ID: 32363839