The role of phosphoinositides in membrane transport

Simonsen, Anne; Wurmser, Andrew E.; Emr, Scott D.; Stenmark, Harald

doi:10.1016/s0955-0674(00)00240-4

Cited by 442 publications

(370 citation statements)

References 60 publications

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“…Thus, EpsinR2 may be recruited to a specific compartment rich in PtdIns(3)P in plant cells, as suggested previously for other epsin-related proteins (Itoh et al, 2001;Friant et al, 2003;Hirst et al, 2003). Similar to its role in animal and yeast cells (Wurmser and Emr, 1998;Gillooly et al, 2000;Simonsen et al, 2001), PtdIns(3)P plays a critical role in vacuolar trafficking in plant cells (Kim et al, 2001a). Both the PtdIns(3)P-specific binding domain of early endosome antigen 1 and wortmannin, an inhibitor of PtdIns 3-kinase, strongly suppress vacuolar trafficking at the Golgi complex in BY-2 and Arabidopsis leaf cells (Matsuoka et al,1995;Kim et al, 2001a), and wortmannin treatment affects MBV formation in plant cells (Tse et al, 2004).…”

Section: Discussion Binding Partners Of Epsinr2supporting

confidence: 54%

“…The localization of EpsinR2 to the d compartment was strongly dependent on an intact ENTH domain. This result suggested that the d compartment is rich in PtdIns(3)P. Previous studies have shown that PtdIns(3)P plays a critical role in protein trafficking from endosomes in both animal and plant cells (Wurmser and Emr, 1998;Gillooly et al, 2000;Kim et al, 2001a;Simonsen et al, 2001). In animal cells, AP-3 is located in endosomes (Peden et al, 2004).…”

Section: Localization Of Epsinr2mentioning

confidence: 79%

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EpsinR2 Interacts with Clathrin, Adaptor Protein-3, AtVTI12, and Phosphatidylinositol-3-Phosphate. Implications for EpsinR2 Function in Protein Trafficking in Plant Cells

et al. 2007

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Members of the epsin family of proteins (epsins) are characterized by the presence of an epsin N-terminal homology (ENTH) domain. Epsins have been implicated in various protein-trafficking pathways in animal and yeast (Saccharomyces cerevisiae) cells. Plant cells also contain multiple epsin-related proteins. In Arabidopsis (Arabidopsis thaliana), EPSIN1 is involved in vacuolar trafficking of soluble proteins. In this study, we investigated the role of Arabidopsis EpsinR2 in protein trafficking in plant cells. EpsinR2 contains a highly conserved ENTH domain but a fairly divergent C-terminal sequence. We found that the N-terminal ENTH domain specifically binds to phosphatidylinositol-3-P in vitro and has a critical role in the targeting of EpsinR2. Upon transient expression in protoplasts, hemagglutinin epitope-tagged EpsinR2 was translocated primarily to a novel cellular compartment, while a minor portion localized to the Golgi complex. Protein-binding experiments showed that EpsinR2 interacts with clathrin, AtVTI12, and the Arabidopsis homologs of adaptor protein-3 d-adaptin and adaptor protein-2 a-adaptin. Localization experiments revealed that hemagglutinin epitope-tagged EpsinR2 colocalizes primarily with d-adaptin and partially colocalizes with clathrin and AtVTI12. Based on these findings, we propose that EpsinR2 plays an important role in protein trafficking through interactions with d-adaptin, AtVTI12, clathrin, and phosphatidylinositol-3-P.

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Section: Discussion Binding Partners Of Epsinr2supporting

confidence: 54%

Section: Localization Of Epsinr2mentioning

confidence: 79%

EpsinR2 Interacts with Clathrin, Adaptor Protein-3, AtVTI12, and Phosphatidylinositol-3-Phosphate. Implications for EpsinR2 Function in Protein Trafficking in Plant Cells

et al. 2007

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“…Similar to animal cells, clathrin-mediated endocytosis in plants is likely to be linked to phosphoinositide signaling (Simonsen et al, 2001;Lee et al, 2007). In agreement with this, phosphoinositides have been implicated in cell plate maturation.…”

Section: Vesicle Trafficking Involved In Cell Plate Maturationmentioning

confidence: 59%

Vesicle Trafficking during Somatic Cytokinesis

2008

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“…The PI 3-kinase inhibitor wortmannin inhibits the synthesis of PtdIns(3)P, resulting in enlarged endosomes. (Simonsen et al, 2001). Because wortmannin inhibits both class I and III PI 3-kinases, which synthesize PtdIns(3)P, PtdIns(3,4)P 2 , PtdIns(3,4,5)P 3 , and PtdIns(3,5)P 2 , dissection of the trafficking pathways regulated by each specific phosphoinositide has not been directly evaluated.…”

Section: Discussionmentioning

confidence: 99%

The Type Iα Inositol Polyphosphate 4-Phosphatase Generates and Terminates Phosphoinositide 3-Kinase Signals on Endosomes and the Plasma Membrane

Ivetac

Munday

Kisseleva

et al. 2005

MBoC

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Endosomal trafficking is regulated by the recruitment of effector proteins to phosphatidylinositol 3-phosphate [PtdIns(3)P] on early endosomes. At the plasma membrane, phosphatidylinositol-(3,4)-bisphosphate [PtdIns(3,4)P2] binds the pleckstrin homology (PH) domain-containing proteins Akt and TAPP1. Type Iα inositol polyphosphate 4-phosphatase (4-phosphatase) dephosphorylates PtdIns(3,4)P2, forming PtdIns(3)P, but its subcellular localization is unknown. We report here in quiescent cells, the 4-phosphatase colocalized with early and recycling endosomes. On growth factor stimulation, 4-phosphatase endosomal localization persisted, but in addition the 4-phosphatase localized at the plasma membrane. Overexpression of the 4-phosphatase in serum-stimulated cells increased cellular PtdIns(3)P levels and prevented wortmannin-induced endosomal dilatation. Furthermore, mouse embryonic fibroblasts from homozygous Weeble mice, which have a mutation in the type I 4-phosphatase, exhibited dilated early endosomes. 4-Phosphatase translocation to the plasma membrane upon growth factor stimulation inhibited the recruitment of the TAPP1 PH domain. The 4-phosphatase contains C2 domains, which bound PtdIns(3,4)P2, and C2-domain-deletion mutants lost PtdIns(3,4)P2 4-phosphatase activity, did not localize to endosomes or inhibit TAPP1 PH domain membrane recruitment. The 4-phosphatase therefore both generates and terminates phosphoinositide 3-kinase signals at distinct subcellular locations.

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The role of phosphoinositides in membrane transport

Cited by 442 publications

References 60 publications

EpsinR2 Interacts with Clathrin, Adaptor Protein-3, AtVTI12, and Phosphatidylinositol-3-Phosphate. Implications for EpsinR2 Function in Protein Trafficking in Plant Cells

EpsinR2 Interacts with Clathrin, Adaptor Protein-3, AtVTI12, and Phosphatidylinositol-3-Phosphate. Implications for EpsinR2 Function in Protein Trafficking in Plant Cells

Vesicle Trafficking during Somatic Cytokinesis

The Type Iα Inositol Polyphosphate 4-Phosphatase Generates and Terminates Phosphoinositide 3-Kinase Signals on Endosomes and the Plasma Membrane

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