Determinants for <i>Arabidopsis</i> Peptide Transporter Targeting to the Tonoplast or Plasma Membrane

Komarova, Nataliya Y.; Meier, Stefan; Meier, Anna; Grotemeyer, Marianne Suter; Rentsch, Doris

doi:10.1111/j.1600-0854.2012.01370.x

Cited by 49 publications

(50 citation statements)

References 83 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As inferred from the transcriptional activation of the corresponding genes in cells containing arbuscules (Table S3), both MtPTR1 and MtSPT13 are likely to have a role at this symbiotic interface. According to characterization of the PMlocalized PTR1 in Arabidopsis (Komorova et al 2008(Komorova et al , 2012, MtPTR1 may function as a di-and tripeptide transporter. Noticeably, the putative dipeptide transporter RiPTR2 has been identified in R. irregularis (Belmondo et al 2014).…”

Section: Am-responsive Proteins As Related To Sugar/peptide Transportmentioning

confidence: 99%

The plasma membrane proteome of Medicago truncatula roots as modified by arbuscular mycorrhizal symbiosis

Aloui¹,

Recorbet²,

Lemaître‐Guillier³

et al. 2017

Mycorrhiza

View full text Add to dashboard Cite

In arbuscular mycorrhizal (AM) roots, the plasma membrane (PM) of the host plant is involved in all developmental stages of the symbiotic interaction, from initial recognition to intracellular accommodation of intra-radical hyphae and arbuscules. Although the role of the PM as the agent for cellular morphogenesis and nutrient exchange is especially accentuated in endosymbiosis, very little is known regarding the PM protein composition of mycorrhizal roots. To obtain a global overview at the proteome level of the host PM proteins as modified by symbiosis, we performed a comparative protein profiling of PM fractions from Medicago truncatula roots either inoculated or not with the AM fungus Rhizophagus irregularis. PM proteins were isolated from root microsomes using an optimized discontinuous sucrose gradient; their subsequent analysis by liquid chromatography followed by mass spectrometry (MS) identified 674 proteins. Cross-species sequence homology searches combined with MS-based quantification clearly confirmed enrichment in PM-associated proteins and depletion of major microsomal contaminants. Changes in protein amounts between the PM proteomes of mycorrhizal and non-mycorrhizal roots were monitored further by spectral counting. This workflow identified a set of 82 mycorrhiza-responsive proteins that provided insights into the plant PM response to mycorrhizal symbiosis. Among them, the association of one third of the mycorrhiza-responsive proteins with detergent-resistant membranes pointed at partitioning to PM microdomains. The PM-associated proteins responsive to mycorrhization also supported host plant control of sugar uptake to limit fungal colonization, and lipid turnover events in the PM fraction of symbiotic roots. Because of the depletion upon symbiosis of proteins mediating the replacement of phospholipids by phosphorus-free lipids in the plasmalemma, we propose a role of phosphate nutrition in the PM composition of mycorrhizal roots.

show abstract

Section: Am-responsive Proteins As Related To Sugar/peptide Transportmentioning

confidence: 99%

The plasma membrane proteome of Medicago truncatula roots as modified by arbuscular mycorrhizal symbiosis

Aloui¹,

Recorbet²,

Lemaître‐Guillier³

et al. 2017

Mycorrhiza

View full text Add to dashboard Cite

show abstract

“…Consequently, mutation of the dileucine signal will block the interaction further exposing the PM targeting signal to the surface. Actually, a study with the PM protein H + -ATPase in tobacco (Nicotiana tabacum) indicated that one large loop between TMDs is essential for its PM localization, similar to the case of the PM proteins PTR1 and PTR5, whereas the first TMD of SCAMP1 has been shown to be essential for its TGN-PM targeting (Lefebvre et al, 2004;Cai et al, 2011;Komarova et al, 2012). These studies then question whether the default pathway exists for all proteins.…”

Section: Mutation Of Tonoplast Sorting Signal Results In Pm Localizationmentioning

confidence: 99%

“…INT1 was reported to be a tonoplast transporter with a dileucine motif at its C terminus (Komarova et al, 2012;Larisch et al, 2012;Wolfenstetter et al, 2012). Indeed, GFP-INT1 labeled the tonoplast in the wild-type plant ( Figure 8D).…”

Section: Tonoplast Targeting Of Dileucine Motif-containing Proteins Imentioning

confidence: 99%

“…Another study with Arabidopsis b-Fructosidase 4 has identified EEE and LCPYTRL sequence motifs as sorting signals on the way from the TGN to the central vacuole (Jung et al, 2011). Similar to cases in mammalian cells and yeast, a conserved dileucine motif is also involved in the targeting of tonoplast membrane proteins in plant cells, as recorded for several proteins like the monosaccharide transporter ERD SIX-LIKE1 (ESL1), the molybdate transporter2 (MOT2), two pore channel1 (TPC1), peptide transporter1 (PTR1), and inositol transporter1 (INT1) (Yamada et al, 2010;Gasber et al, 2011;Komarova et al, 2012;Larisch et al, 2012;Wolfenstetter et al, 2012). However, more precise information on the underlying mechanism is lacking.…”

Section: Introductionmentioning

confidence: 99%

“…Beyond the Golgi apparatus, proteins need additional sorting signals for correct tonoplast targeting. Recently, several studies reported on the dileucine motif in plant, which was also found in the N terminus of VIT1 (EKQTLL) (Komarova et al, 2012;Larisch et al, 2012;Wolfenstetter et al, 2012). To test whether this putative motif is functional, we further mutated the conserved amino acids (glutamic acid and leucine) to alanine in this motif ( Figure 3A).…”

Section: The N Terminus Of Vit1 Contains a Dileucine Motif For Tonoplmentioning

confidence: 99%

See 2 more Smart Citations

Trans-Golgi Network-Located AP1 Gamma Adaptins Mediate Dileucine Motif-Directed Vacuolar Targeting in Arabidopsis

et al. 2014

View full text Add to dashboard Cite

Membrane proteins on the tonoplast are indispensible for vacuolar functions in plants. However, how these proteins are transported to the vacuole and how they become separated from plasma membrane proteins remain largely unknown. In this study, we used Arabidopsis thaliana vacuolar ion transporter1 (VIT1) as a reporter to study the mechanisms of tonoplast targeting. We showed that VIT1 reached the tonoplast through a pathway involving the endoplasmic reticulum (ER), Golgi, trans-Golgi network (TGN), prevacuolar compartment, and tonoplast. VIT1 contains a putative N-terminal dihydrophobic type ER export signal, and its N terminus has a conserved dileucine motif (EKQTLL), which is responsible for tonoplast targeting. In vitro peptide binding assays with synthetic VIT1 N terminus identified adaptor protein complex-1 (AP1) subunits that interacted with the dileucine motif. A deficiency of AP1 gamma adaptins in Arabidopsis cells caused relocation of tonoplast proteins containing the dileucine motif, such as VIT1 and inositol transporter1, to the plasma membrane. The dileucine motif also effectively rerouted the plasma membrane protein SCAMP1 to the tonoplast. Together with subcellular localization studies showing that AP1 gamma adaptins localize to the TGN, we propose that the AP1 complex on the TGN mediates tonoplast targeting of membrane proteins with the dileucine motif.

show abstract

Vacuole-Targeted Proteins: Ins and Outs of Subcellular Localization Studies

Carqueijeiro¹,

Sepúlveda²,

Mosquera³

et al. 2018

Plant Vacuolar Trafficking

View full text Add to dashboard Cite

Accurate and efficient demonstrations of protein localizations to the vacuole or tonoplast remain strict prerequisites to decipher the role of vacuoles in the whole plant cell biology and notably in defence processes. In this chapter, we describe a reliable procedure of protein subcellular localization study through transient transformations of Catharanthus roseus or onion cells and expression of fusions with fluorescent proteins allowing minimizing artefacts of targeting.

show abstract

Determinants for Arabidopsis Peptide Transporter Targeting to the Tonoplast or Plasma Membrane

Cited by 49 publications

References 83 publications

The plasma membrane proteome of Medicago truncatula roots as modified by arbuscular mycorrhizal symbiosis

The plasma membrane proteome of Medicago truncatula roots as modified by arbuscular mycorrhizal symbiosis

Trans-Golgi Network-Located AP1 Gamma Adaptins Mediate Dileucine Motif-Directed Vacuolar Targeting in Arabidopsis

Vacuole-Targeted Proteins: Ins and Outs of Subcellular Localization Studies

Contact Info

Product

Resources

About