Plasma Membranes Are Subcompartmentalized into a Plethora of Coexisting and Diverse Microdomains in<i>Arabidopsis</i>and<i>Nicotiana benthamiana</i>

Jarsch, Iris K.; Konrad, Sebastian S. A.; Stratil, Thomas F.; Urbanus, Susan L.; Szymanski, Witold G.; Braun, Pascal; Braun, Karl-Heinz; Ott, Thomas

doi:10.1105/tpc.114.124446

Cited by 162 publications

(213 citation statements)

References 54 publications

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“…4A). Our data are in agreement with work by Jarsch et al (2014), who reported the formation of PM subdomains in N. benthamiana and Arabidopsis. As expected, GFP-IQD25 fluorescence colocalized upon plasmolysis with the PM and not with the cell wall, which were stained with FM4-64 and propidium iodide (PI), respectively (Fig.…”

Section: A Subset Of Iqd Proteins Localizes To Distinct Pm Subdomainssupporting

confidence: 83%

“…3). Similar patterns have been reported for Rem proteins (Raffaele et al, 2007;Jarsch et al, 2014), and targeting of AtRem6.6 to subdomains in the PM proved to be sensitive to MTdepolymerizing drugs , as was the case for IQD12 and IQD22 (Fig. 3).…”

Section: Discussionsupporting

confidence: 57%

“…These patterns are reminiscent of membrane subdomains, which are largely immobile compartments within the PM (Saka et al, 2014), and thought to serve as platforms of signal transduction (e.g. during immune signaling or polarized growth; Malinsky et al, 2013;Jarsch et al, 2014). We observed similar localization patterns for two PM subdomain marker proteins of the plant-specific REMORIN (Rem) family, Rem6.6 and Rem6.7 , which we included as controls (Fig.…”

Section: A Subset Of Iqd Proteins Localizes To Distinct Pm Subdomainssupporting

confidence: 48%

“…3). Studies in Saccharomyces cerevisiae (yeast) and Arabidopsis revealed that different populations of subdomains coexist in membranes (Spira et al, 2012;Jarsch et al, 2014). Notably, S-acylation appears to play a predominant role for protein anchoring at membrane subdomains in plants (Hemsley and Grierson, 2008), as has been demonstrated for Rho-like GTPases (Craddock et al, 2013) and for plant-specific scaffold proteins of the Rem family Konrad and Ott, 2015).…”

Section: Discussionmentioning

confidence: 99%

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The IQD Family of Calmodulin-Binding Proteins Links Calcium Signaling to Microtubules, Membrane Subdomains, and the Nucleus

et al. 2017

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ORCID IDs: 0000-0002-3493-4800 (K.B.); 0000-0002-7146-043X (B.M.).Calcium (Ca 2+ ) signaling and dynamic reorganization of the cytoskeleton are essential processes for the coordination and control of plant cell shape and cell growth. Calmodulin (CaM) and closely related calmodulin-like (CML) polypeptides are principal sensors of Ca 2+ signals. CaM/CMLs decode and relay information encrypted by the second messenger via differential interactions with a wide spectrum of targets to modulate their diverse biochemical activities. The plant-specific IQ67 DOMAIN (IQD) family emerged as possibly the largest class of CaM-interacting proteins with undefined molecular functions and biological roles. Here, we show that the 33 members of the IQD family in Arabidopsis (Arabidopsis thaliana) differentially localize, using green fluorescent protein (GFP)-tagged proteins, to multiple and distinct subcellular sites, including microtubule (MT) arrays, plasma membrane subdomains, and nuclear compartments. Intriguingly, the various IQD-specific localization patterns coincide with the subcellular patterns of IQD-dependent recruitment of CaM, suggesting that the diverse IQD members sequester Ca 2+ -CaM signaling modules to specific subcellular sites for precise regulation of Ca 2+ -dependent processes. Because MT localization is a hallmark of most IQD family members, we quantitatively analyzed GFP-labeled MT arrays in Nicotiana benthamiana cells transiently expressing GFP-IQD fusions and observed IQD-specific MT patterns, which point to a role of IQDs in MT organization and dynamics. Indeed, stable overexpression of select IQD proteins in Arabidopsis altered cellular MT orientation, cell shape, and organ morphology. Because IQDs share biochemical properties with scaffold proteins, we propose that IQD families provide an assortment of platform proteins for integrating CaM-dependent Ca 2+ signaling at multiple cellular sites to regulate cell function, shape, and growth.

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Section: A Subset Of Iqd Proteins Localizes To Distinct Pm Subdomainssupporting

confidence: 83%

Section: Discussionsupporting

confidence: 57%

Section: A Subset Of Iqd Proteins Localizes To Distinct Pm Subdomainssupporting

confidence: 48%

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

The IQD Family of Calmodulin-Binding Proteins Links Calcium Signaling to Microtubules, Membrane Subdomains, and the Nucleus

et al. 2017

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“…Plant plasma membrane domains have been visualized in vivo using sterol-dependent proteins of the Remorin family [1,2]. The Remorin gene family is unique to plants, found in angiosperms, gymnosperms and bryophytes [3].…”

Section: Introductionmentioning

confidence: 99%

Mobility of Group 1b Remorins in Membrane Nanodomains Differs Significantly between Mesophyll Cells and Protoplasts

JO¹,

Kreuzer²

2015

J Plant Biochem Physiol

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Novel approach to measure the size of plasma‐membrane nanodomains in single molecule localization microscopy

et al. 2015

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Many membrane proteins are not evenly distributed over the plasma membrane, but gathered in domains assumed to have a particular lipid composition. Using single molecule localization microscopy (SMLM) we have immunolocalized a glycosylphosphatidylinositol (GPI)-anchor protein that labels nanodomains in a specialized plant cell type, and compared the suitability of three methods to estimate their size. As conventional methods full width at half maximum (FWHM) and the full diameter (FWMin) of domains were used. A boundary detection method of the domain area (DA) was performed in order to take irregular shapes into account. In order to compare the influence of the chosen measurement methods, we have developed a MatLab program that allows for automated analysis of domain sizes from multiple SMLM images and provides the statistics of three key features of domains: FWHM and FWMin along their long and short axes as well as the DA, derived from the molecular density. Domains formed by the GPI-anchor protein are approximating elliptical shapes. Direct and indirect immunolabeling resulted in a statistically significant difference in apparent domain size, reflecting the fact that the secondary antibody molecules extend the uncertainty along the nanodomain border. FWMin values along the long and short axis give good estimates of regular, geometrically centred domain shapes, while the DA value matches regular as well as irregular shapes best, as derived from computer-generated, irregular point clusters. V C 2015 International Society for Advancement of Cytometry

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Plasma Membranes Are Subcompartmentalized into a Plethora of Coexisting and Diverse Microdomains inArabidopsisandNicotiana benthamiana

Cited by 162 publications

References 54 publications

The IQD Family of Calmodulin-Binding Proteins Links Calcium Signaling to Microtubules, Membrane Subdomains, and the Nucleus

The IQD Family of Calmodulin-Binding Proteins Links Calcium Signaling to Microtubules, Membrane Subdomains, and the Nucleus

Mobility of Group 1b Remorins in Membrane Nanodomains Differs Significantly between Mesophyll Cells and Protoplasts

Novel approach to measure the size of plasma‐membrane nanodomains in single molecule localization microscopy

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