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FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P

Research output: Contribution to journalArticlepeer-review

DOI

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FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P. / Godi, Anna; Di Campli, Antonella; Konstantakopoulos, Athanasios; Di Tullio, Giuseppe; Alessi, Dario R; Kular, Gursant S; Daniele, Tiziana; Marra, Pierfrancesco; Lucocq, John M; De Matteis, M Antonietta.

In: Nature Cell Biology, Vol. 6, No. 5, 05.2004, p. 393-404.

Research output: Contribution to journalArticlepeer-review

Harvard

Godi, A, Di Campli, A, Konstantakopoulos, A, Di Tullio, G, Alessi, DR, Kular, GS, Daniele, T, Marra, P, Lucocq, JM & De Matteis, MA 2004, 'FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P', Nature Cell Biology, vol. 6, no. 5, pp. 393-404. https://doi.org/10.1038/ncb1119

APA

Godi, A., Di Campli, A., Konstantakopoulos, A., Di Tullio, G., Alessi, D. R., Kular, G. S., Daniele, T., Marra, P., Lucocq, J. M., & De Matteis, M. A. (2004). FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P. Nature Cell Biology, 6(5), 393-404. https://doi.org/10.1038/ncb1119

Vancouver

Godi A, Di Campli A, Konstantakopoulos A, Di Tullio G, Alessi DR, Kular GS et al. FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P. Nature Cell Biology. 2004 May;6(5):393-404. https://doi.org/10.1038/ncb1119

Author

Godi, Anna ; Di Campli, Antonella ; Konstantakopoulos, Athanasios ; Di Tullio, Giuseppe ; Alessi, Dario R ; Kular, Gursant S ; Daniele, Tiziana ; Marra, Pierfrancesco ; Lucocq, John M ; De Matteis, M Antonietta. / FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P. In: Nature Cell Biology. 2004 ; Vol. 6, No. 5. pp. 393-404.

Bibtex - Download

@article{58c7b1e4cfcc462b8e39adca60036e22,
title = "FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P",
abstract = "The molecular mechanisms underlying the formation of carriers trafficking from the Golgi complex to the cell surface are still ill-defined; nevertheless, the involvement of a lipid-based machinery is well established. This includes phosphatidylinositol 4-phosphate (PtdIns(4)P), the precursor for phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P(2)). In yeast, PtdIns(4)P exerts a direct role, however, its mechanism of action and its targets in mammalian cells remain uncharacterized. We have identified two effectors of PtdIns(4)P, the four-phosphate-adaptor protein 1 and 2 (FAPP1 and FAPP2). Both proteins localize to the trans-Golgi network (TGN) on nascent carriers, and interact with PtdIns(4)P and the small GTPase ADP-ribosylation factor (ARF) through their plekstrin homology (PH) domain. Displacement or knockdown of FAPPs inhibits cargo transfer to the plasma membrane. Moreover, overexpression of FAPP-PH impairs carrier fission. Therefore, FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery that controls generation of constitutive post-Golgi carriers.",
keywords = "ADP-Ribosylation Factors, Adaptor Proteins, Signal Transducing, Animals, Biological Transport, COS Cells, Carrier Proteins, Cell Membrane, Fungal Proteins, Golgi Apparatus, Humans, Molecular Sequence Data, Phosphatidylinositol Phosphates, Protein Structure, Tertiary, RNA, Small Interfering, Recombinant Fusion Proteins, Subcellular Fractions, trans-Golgi Network",
author = "Anna Godi and {Di Campli}, Antonella and Athanasios Konstantakopoulos and {Di Tullio}, Giuseppe and Alessi, {Dario R} and Kular, {Gursant S} and Tiziana Daniele and Pierfrancesco Marra and Lucocq, {John M} and {De Matteis}, {M Antonietta}",
year = "2004",
month = may,
doi = "10.1038/ncb1119",
language = "English",
volume = "6",
pages = "393--404",
journal = "Nature Cell Biology",
issn = "1465-7392",
publisher = "Nature publishing group",
number = "5",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P

AU - Godi, Anna

AU - Di Campli, Antonella

AU - Konstantakopoulos, Athanasios

AU - Di Tullio, Giuseppe

AU - Alessi, Dario R

AU - Kular, Gursant S

AU - Daniele, Tiziana

AU - Marra, Pierfrancesco

AU - Lucocq, John M

AU - De Matteis, M Antonietta

PY - 2004/5

Y1 - 2004/5

N2 - The molecular mechanisms underlying the formation of carriers trafficking from the Golgi complex to the cell surface are still ill-defined; nevertheless, the involvement of a lipid-based machinery is well established. This includes phosphatidylinositol 4-phosphate (PtdIns(4)P), the precursor for phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P(2)). In yeast, PtdIns(4)P exerts a direct role, however, its mechanism of action and its targets in mammalian cells remain uncharacterized. We have identified two effectors of PtdIns(4)P, the four-phosphate-adaptor protein 1 and 2 (FAPP1 and FAPP2). Both proteins localize to the trans-Golgi network (TGN) on nascent carriers, and interact with PtdIns(4)P and the small GTPase ADP-ribosylation factor (ARF) through their plekstrin homology (PH) domain. Displacement or knockdown of FAPPs inhibits cargo transfer to the plasma membrane. Moreover, overexpression of FAPP-PH impairs carrier fission. Therefore, FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery that controls generation of constitutive post-Golgi carriers.

AB - The molecular mechanisms underlying the formation of carriers trafficking from the Golgi complex to the cell surface are still ill-defined; nevertheless, the involvement of a lipid-based machinery is well established. This includes phosphatidylinositol 4-phosphate (PtdIns(4)P), the precursor for phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P(2)). In yeast, PtdIns(4)P exerts a direct role, however, its mechanism of action and its targets in mammalian cells remain uncharacterized. We have identified two effectors of PtdIns(4)P, the four-phosphate-adaptor protein 1 and 2 (FAPP1 and FAPP2). Both proteins localize to the trans-Golgi network (TGN) on nascent carriers, and interact with PtdIns(4)P and the small GTPase ADP-ribosylation factor (ARF) through their plekstrin homology (PH) domain. Displacement or knockdown of FAPPs inhibits cargo transfer to the plasma membrane. Moreover, overexpression of FAPP-PH impairs carrier fission. Therefore, FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery that controls generation of constitutive post-Golgi carriers.

KW - ADP-Ribosylation Factors

KW - Adaptor Proteins, Signal Transducing

KW - Animals

KW - Biological Transport

KW - COS Cells

KW - Carrier Proteins

KW - Cell Membrane

KW - Fungal Proteins

KW - Golgi Apparatus

KW - Humans

KW - Molecular Sequence Data

KW - Phosphatidylinositol Phosphates

KW - Protein Structure, Tertiary

KW - RNA, Small Interfering

KW - Recombinant Fusion Proteins

KW - Subcellular Fractions

KW - trans-Golgi Network

U2 - 10.1038/ncb1119

DO - 10.1038/ncb1119

M3 - Article

C2 - 15107860

VL - 6

SP - 393

EP - 404

JO - Nature Cell Biology

JF - Nature Cell Biology

SN - 1465-7392

IS - 5

ER -

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