The Intrinsically Disordered N-terminal Region of AtREM1.3 Remorin Protein Mediates Protein-Protein Interactions

Marín, Macarena; Thallmair, Veronika; Ott, Thomas

doi:10.1074/jbc.m112.414292

Cited by 69 publications

(50 citation statements)

References 57 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…More detail for the interacting proteins can be found in Supplemental Table S2. (Table continues on following page.) the remorin proteins REMORIN1.2 (REM1.2) and REM1.3 (Borner et al, 2005;Marín et al, 2012). A recent study (Levy et al, 2015) demonstrated that SYTA forms ER-PM junctions that are specifically recruited to PD during virus movement.…”

Section: Validation Of the Proteomics Approachmentioning

confidence: 99%

“…The tomato (Solanum lycopersicum) REM1.3 is required for the restriction of potato virus X trafficking (Perraki et al, 2012), while the potato REM1.3 affects the ability of the TRIPLE GENE BLOCK1 MP of Potato virus X and other viral MPs to increase PD permeability (Perraki et al, 2014). Several remorins, including Arabidopsis REM1.3, form nonamyloid filamentous structures of 5.7 to 8 nm (Bariola et al, 2004;Marín et al, 2012). These remorins could be linked with the cytoskeleton in superstructures to maintain cell integrity or act as scaffold proteins for signaling and defense mechanisms (Bariola et al, 2004), a process that might occur in combination with the structural RTNLB proteins.…”

Section: Validation Of the Proteomics Approachmentioning

confidence: 99%

See 1 more Smart Citation

Reticulomics: Protein-protein interaction studies with two plasmodesmata-localised reticulon family proteins identify binding partners enriched at plasmodesmata, ER and the plasma membrane

et al. 2015

View full text Add to dashboard Cite

The endoplasmic reticulum (ER) is a ubiquitous organelle that plays roles in secretory protein production, folding, quality control, and lipid biosynthesis. The cortical ER in plants is pleomorphic and structured as a tubular network capable of morphing into flat cisternae, mainly at three-way junctions, and back to tubules. Plant reticulon family proteins (RTNLB) tubulate the ER by dimerization and oligomerization, creating localized ER membrane tensions that result in membrane curvature. Some RTNLB ER-shaping proteins are present in the plasmodesmata (PD) proteome and may contribute to the formation of the desmotubule, the axial ER-derived structure that traverses primary PD. Here, we investigate the binding partners of two PD-resident reticulon proteins, RTNLB3 and RTNLB6, that are located in primary PD at cytokinesis in tobacco (Nicotiana tabacum). Coimmunoprecipitation of green fluorescent protein-tagged RTNLB3 and RTNLB6 followed by mass spectrometry detected a high percentage of known PD-localized proteins as well as plasma membrane proteins with putative membrane-anchoring roles. Förster resonance energy transfer by fluorescence lifetime imaging microscopy assays revealed a highly significant interaction of the detected PD proteins with the bait RTNLB proteins. Our data suggest that RTNLB proteins, in addition to a role in ER modeling, may play important roles in linking the cortical ER to the plasma membrane.The endoplasmic reticulum (ER) is a multifunctional organelle and is the site of secretory protein production, folding, and quality control (Brandizzi et al., 2003) and lipid biosynthesis (Wallis and Browse, 2010), but it is also involved in many other aspects of day-to-day plant life, including auxin regulation (Friml and Jones, 2010) and oil and protein body formation (Huang, 1996;Herman, 2008). The cortical ER network displays a remarkable polygonal arrangement of motile tubules that are capable of morphing into small cisternae, mainly at the three-way junctions of the ER network (Sparkes et al., 2009). The cortical ER network of plants has been shown to play multiple roles in protein trafficking (Palade, 1975;Vitale and Denecke, 1999) and pathogen responses (for review, see Pattison and Amtmann, 2009;Beck et al., 2012).In plants, the protein family of reticulons (RTNLBs) contributes significantly to tubulation of the ER (Tolley et al., 2008Chen et al., 2012). RTNLBs are integral ER membrane proteins that feature a C-terminal reticulon homology domain (RHD) that contains two major hydrophobic regions. These regions form two V-shaped transmembrane wedges joined together via a cytosolic loop, with the C and N termini of the protein facing the cytosol. RTNLBs can dimerize or oligomerize, creating localized tensions in the ER membrane, inducing varying degrees of membrane curvature . Hence, RTNLBs are considered to be essential in maintaining the tubular ER network.The ability of RTNLBs to constrict membranes is of interest in the context of cell plate development and the formation of primary plasmo...

show abstract

Section: Validation Of the Proteomics Approachmentioning

confidence: 99%

Section: Validation Of the Proteomics Approachmentioning

confidence: 99%

Reticulomics: Protein-protein interaction studies with two plasmodesmata-localised reticulon family proteins identify binding partners enriched at plasmodesmata, ER and the plasma membrane

et al. 2015

View full text Add to dashboard Cite

show abstract

“…Phosphorylation state is also known to play an important regulatory role in protein-protein interactions (Marín et al, 2012;Orr, 2012;Ebert et al, 2013). E. coli MscS forms a homoheptameric channel (Bass et al, 2002;Miller et al, 2003a), and MSL10 is likely to form a multimer as well.…”

Section: Preventing or Mimicking Phosphorylation Of The Msl10 N-termimentioning

confidence: 99%

Arabidopsis MSL10 Has a Regulated Cell Death Signaling Activity That Is Separable from Its Mechanosensitive Ion Channel Activity

et al. 2014

View full text Add to dashboard Cite

Members of the MscS superfamily of mechanosensitive ion channels function as osmotic safety valves, releasing osmolytes under increased membrane tension. MscS homologs exhibit diverse topology and domain structure, and it has been proposed that the more complex members of the family might have novel regulatory mechanisms or molecular functions. Here, we present a study of MscS-Like (MSL)10 from Arabidopsis thaliana that supports these ideas. High-level expression of MSL10-GFP in Arabidopsis induced small stature, hydrogen peroxide accumulation, ectopic cell death, and reactive oxygen species-and cell death-associated gene expression. Phosphomimetic mutations in the MSL10 N-terminal domain prevented these phenotypes. The phosphorylation state of MSL10 also regulated its ability to induce cell death when transiently expressed in Nicotiana benthamiana leaves but did not affect subcellular localization, assembly, or channel behavior. Finally, the N-terminal domain of MSL10 was sufficient to induce cell death in tobacco, independent of phosphorylation state. We conclude that the plant-specific N-terminal domain of MSL10 is capable of inducing cell death, this activity is regulated by phosphorylation, and MSL10 has two separable activities-one as an ion channel and one as an inducer of cell death. These findings further our understanding of the evolution and significance of mechanosensitive ion channels.

show abstract

“…The presence of trifluoroethanol (TFE) simulates the hydrophobic condition that can arise upon forming protein-protein interaction and has been used to assess the propensity of IDRs to undergo induced folding (Sun et al, 2010;Marín et al, 2012). The N-terminal domain of BnaDGAT1 was titrated with increasing amounts of TFE followed by CD analysis (Fig.…”

Section: The Bnadgat1 N-terminal Domain Is Not Necessary For Catalysimentioning

confidence: 99%

Diacylglycerol Acyltransferase 1 Is Regulated by Its N-Terminal Domain in Response to Allosteric Effectors

et al. 2017

View full text Add to dashboard Cite

ORCID IDs: 0000-0001-8699-690X (R.J.W.); 0000-0003-4745-9153 (M.J.L.).Diacylglycerol acyltransferase 1 (DGAT1) is an integral membrane enzyme catalyzing the final and committed step in the acylcoenzyme A (CoA)-dependent biosynthesis of triacylglycerol (TAG). The biochemical regulation of TAG assembly remains one of the least understood areas of primary metabolism to date. Here, we report that the hydrophilic N-terminal domain of Brassica napus DGAT1 (BnaDGAT1 1-113 ) regulates activity based on acyl-CoA/CoA levels. The N-terminal domain is not necessary for acyltransferase activity and is composed of an intrinsically disordered region and a folded segment. We show that the disordered region has an autoinhibitory function and a dimerization interface, which appears to mediate positive cooperativity, whereas the folded segment of the cytosolic region was found to have an allosteric site for acyl-CoA/CoA. Under increasing acyl-CoA levels, the binding of acyl-CoA with this noncatalytic site facilitates homotropic allosteric activation. Enzyme activation, on the other hand, is prevented under limiting acyl-CoA conditions (low acyl-CoA-to-CoA ratio), whereby CoA acts as a noncompetitive feedback inhibitor through interaction with the same folded segment. The three-dimensional NMR solution structure of the allosteric site revealed an a-helix with a loop connecting a coil fragment. The conserved amino acid residues in the loop interacting with CoA were identified, revealing details of this important regulatory element for allosteric regulation. Based on these results, a model is proposed illustrating the role of the N-terminal domain of BnaDGAT1 as a positive and negative modulator of TAG biosynthesis.

show abstract

The Intrinsically Disordered N-terminal Region of AtREM1.3 Remorin Protein Mediates Protein-Protein Interactions

Cited by 69 publications

References 57 publications

Reticulomics: Protein-protein interaction studies with two plasmodesmata-localised reticulon family proteins identify binding partners enriched at plasmodesmata, ER and the plasma membrane

Reticulomics: Protein-protein interaction studies with two plasmodesmata-localised reticulon family proteins identify binding partners enriched at plasmodesmata, ER and the plasma membrane

Arabidopsis MSL10 Has a Regulated Cell Death Signaling Activity That Is Separable from Its Mechanosensitive Ion Channel Activity

Diacylglycerol Acyltransferase 1 Is Regulated by Its N-Terminal Domain in Response to Allosteric Effectors

Contact Info

Product

Resources

About