The acyltransferase LYCAT controls specific phosphoinositides and related membrane traffic

Leslie N. Bone; Roya M. Dayam; Minhyoung Lee; Nozomu Kono; Gregory D. Fairn; Hiroyuki Arai; Roberto J. Botelho; Costin N. Antonescu

doi:10.1091/mbc.E16-09-0668

The acyltransferase LYCAT controls specific phosphoinositides and related membrane traffic

Leslie N. Bone, Roya M. Dayam, Minhyoung Lee, Nozomu Kono, Gregory D. Fairn, Hiroyuki Arai, Roberto J. Botelho, Costin N. Antonescu

Résultat de recherche: Article › examen par les pairs

33 Citations (Scopus)

Résumé

Phosphoinositides (PIPs) are key regulators of membrane traffic and signaling. The interconversion of PIPs by lipid kinases and phosphatases regulates their functionality. Phosphatidylinositol (PI) and PIPs have a unique enrichment of 1-stearoyl-2-arachidonyl acyl species; however, the regulation and function of this specific acyl profile remains poorly understood. We examined the role of the PI acyltransferase LYCAT in control of PIPs and PIP-dependent membrane traffic. LYCAT silencing selectively perturbed the levels and localization of phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] and phosphatidylinositol-3-phosphate and the membrane traffic dependent on these specific PIPs but was without effect on phosphatidylinositol-4-phosphate or biosynthetic membrane traffic. The acyl profile of PI(4,5)P2 was selectively altered in LYCAT-deficient cells, whereas LYCAT localized with phosphatidylinositol synthase. We propose that LYCAT remodels the acyl chains of PI, which is then channeled into PI(4,5)P2. Our observations suggest that the PIP acyl chain profile may exert broad control of cell physiology.

Langue d'origine	English
Pages (de-à)	161-172
Nombre de pages	12
Journal	Molecular Biology of the Cell
Volume	28
Numéro de publication	1
DOI	https://doi.org/10.1091/mbc.E16-09-0668
Statut de publication	Published - janv. 1 2017
Publié à l'externe	Oui

Note bibliographique

Funding Information:
We thank T. Balla for the kind gifts of the plasmids encoding eGFP-PIS and eGFP-P4M and P. de Camilli for the kind gift of the plasmid encoding eGFP-E-Sty2. This work was supported by an Ontario Early Researcher Award, a Canada Research Chair Award, and a Natural Sciences and Engineering Research Council Grant to R.J.B and a Ryerson Health Research Fund Award and an Operating Grant from the Canadian Institutes of Health Research (Grant 125854) to C.N.A. L.N.B was supported in part by an Ontario Graduate Scholarship.

Publisher Copyright:
© 2017 Bone et al.

ASJC Scopus Subject Areas

Molecular Biology
Cell Biology

Accès au document

10.1091/mbc.E16-09-0668

Autres fichiers et liens

Citer

@article{fc4eeaa604e442cf8d49450d215abf39,

title = "The acyltransferase LYCAT controls specific phosphoinositides and related membrane traffic",

abstract = "Phosphoinositides (PIPs) are key regulators of membrane traffic and signaling. The interconversion of PIPs by lipid kinases and phosphatases regulates their functionality. Phosphatidylinositol (PI) and PIPs have a unique enrichment of 1-stearoyl-2-arachidonyl acyl species; however, the regulation and function of this specific acyl profile remains poorly understood. We examined the role of the PI acyltransferase LYCAT in control of PIPs and PIP-dependent membrane traffic. LYCAT silencing selectively perturbed the levels and localization of phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] and phosphatidylinositol-3-phosphate and the membrane traffic dependent on these specific PIPs but was without effect on phosphatidylinositol-4-phosphate or biosynthetic membrane traffic. The acyl profile of PI(4,5)P2 was selectively altered in LYCAT-deficient cells, whereas LYCAT localized with phosphatidylinositol synthase. We propose that LYCAT remodels the acyl chains of PI, which is then channeled into PI(4,5)P2. Our observations suggest that the PIP acyl chain profile may exert broad control of cell physiology.",

author = "Bone, {Leslie N.} and Dayam, {Roya M.} and Minhyoung Lee and Nozomu Kono and Fairn, {Gregory D.} and Hiroyuki Arai and Botelho, {Roberto J.} and Antonescu, {Costin N.}",

note = "Funding Information: We thank T. Balla for the kind gifts of the plasmids encoding eGFP-PIS and eGFP-P4M and P. de Camilli for the kind gift of the plasmid encoding eGFP-E-Sty2. This work was supported by an Ontario Early Researcher Award, a Canada Research Chair Award, and a Natural Sciences and Engineering Research Council Grant to R.J.B and a Ryerson Health Research Fund Award and an Operating Grant from the Canadian Institutes of Health Research (Grant 125854) to C.N.A. L.N.B was supported in part by an Ontario Graduate Scholarship. Publisher Copyright: {\textcopyright} 2017 Bone et al.",

year = "2017",

month = jan,

day = "1",

doi = "10.1091/mbc.E16-09-0668",

language = "English",

volume = "28",

pages = "161--172",

journal = "Molecular Biology of the Cell",

issn = "1059-1524",

publisher = "American Society for Cell Biology",

number = "1",

}

TY - JOUR

T1 - The acyltransferase LYCAT controls specific phosphoinositides and related membrane traffic

AU - Bone, Leslie N.

AU - Dayam, Roya M.

AU - Lee, Minhyoung

AU - Kono, Nozomu

AU - Fairn, Gregory D.

AU - Arai, Hiroyuki

AU - Botelho, Roberto J.

AU - Antonescu, Costin N.

N1 - Funding Information: We thank T. Balla for the kind gifts of the plasmids encoding eGFP-PIS and eGFP-P4M and P. de Camilli for the kind gift of the plasmid encoding eGFP-E-Sty2. This work was supported by an Ontario Early Researcher Award, a Canada Research Chair Award, and a Natural Sciences and Engineering Research Council Grant to R.J.B and a Ryerson Health Research Fund Award and an Operating Grant from the Canadian Institutes of Health Research (Grant 125854) to C.N.A. L.N.B was supported in part by an Ontario Graduate Scholarship. Publisher Copyright: © 2017 Bone et al.

PY - 2017/1/1

Y1 - 2017/1/1

N2 - Phosphoinositides (PIPs) are key regulators of membrane traffic and signaling. The interconversion of PIPs by lipid kinases and phosphatases regulates their functionality. Phosphatidylinositol (PI) and PIPs have a unique enrichment of 1-stearoyl-2-arachidonyl acyl species; however, the regulation and function of this specific acyl profile remains poorly understood. We examined the role of the PI acyltransferase LYCAT in control of PIPs and PIP-dependent membrane traffic. LYCAT silencing selectively perturbed the levels and localization of phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] and phosphatidylinositol-3-phosphate and the membrane traffic dependent on these specific PIPs but was without effect on phosphatidylinositol-4-phosphate or biosynthetic membrane traffic. The acyl profile of PI(4,5)P2 was selectively altered in LYCAT-deficient cells, whereas LYCAT localized with phosphatidylinositol synthase. We propose that LYCAT remodels the acyl chains of PI, which is then channeled into PI(4,5)P2. Our observations suggest that the PIP acyl chain profile may exert broad control of cell physiology.

AB - Phosphoinositides (PIPs) are key regulators of membrane traffic and signaling. The interconversion of PIPs by lipid kinases and phosphatases regulates their functionality. Phosphatidylinositol (PI) and PIPs have a unique enrichment of 1-stearoyl-2-arachidonyl acyl species; however, the regulation and function of this specific acyl profile remains poorly understood. We examined the role of the PI acyltransferase LYCAT in control of PIPs and PIP-dependent membrane traffic. LYCAT silencing selectively perturbed the levels and localization of phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] and phosphatidylinositol-3-phosphate and the membrane traffic dependent on these specific PIPs but was without effect on phosphatidylinositol-4-phosphate or biosynthetic membrane traffic. The acyl profile of PI(4,5)P2 was selectively altered in LYCAT-deficient cells, whereas LYCAT localized with phosphatidylinositol synthase. We propose that LYCAT remodels the acyl chains of PI, which is then channeled into PI(4,5)P2. Our observations suggest that the PIP acyl chain profile may exert broad control of cell physiology.

UR - http://www.scopus.com/inward/record.url?scp=85008235300&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85008235300&partnerID=8YFLogxK

U2 - 10.1091/mbc.E16-09-0668

DO - 10.1091/mbc.E16-09-0668

M3 - Article

C2 - 28035047

AN - SCOPUS:85008235300

SN - 1059-1524

VL - 28

SP - 161

EP - 172

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

IS - 1

ER -

The acyltransferase LYCAT controls specific phosphoinositides and related membrane traffic

Résumé

Note bibliographique

ASJC Scopus Subject Areas

Accès au document

Autres fichiers et liens

Empreinte numérique

Citer