MTV proteins unveil ER- and microtubule-associated compartments in the plant vacuolar trafficking pathway

Delgadillo, María Otilia; Ruano, Guillermo; Zouhar, Jan; Sauer, Michael; Shen, Jinbo; Lazarova, Aleksandra; Sanmartín, Maite; Lai, Louis Tung Faat; Deng, Cesi; Wang, Pengwei; Hussey, Patrick J.; Sánchez‐Serrano, José J.; Jiang, Liwen; Rojo, Enrique

doi:10.1073/pnas.1919820117

Cited by 25 publications

(26 citation statements)

References 89 publications

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“…Contributions of both actin and microtubule cytoskeletons have also been described in the context of organizing the edge-directed secretory route mediated by RabA5c. Microtubules might also be involved in controlling trafficking rates to different subcellular domains as revealed by PIN2 recycling [ 46 ].…”

Section: Discussionmentioning

confidence: 99%

Actin and Microtubules Differently Contribute to Vacuolar Targeting Specificity during the Export from the ER

et al. 2021

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Plants rely on both actin and microtubule cytoskeletons to fine-tune sorting and spatial targeting of membranes during cell growth and stress adaptation. Considerable advances have been made in recent years in the comprehension of the relationship between the trans-Golgi network/early endosome (TGN/EE) and cytoskeletons, but studies have mainly focused on the transport to and from the plasma membrane. We address here the relationship of the cytoskeleton with different endoplasmic reticulum (ER) export mechanisms toward vacuoles. These emergent features of the plant endomembrane traffic are explored with an in vivo approach, providing clues on the traffic regulation at different levels beyond known proteins’ functions and interactions. We show how traffic of vacuolar markers, characterized by different vacuolar sorting determinants, diverges at the export from the ER, clearly involving different components of the cytoskeleton.

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Section: Discussionmentioning

confidence: 99%

Actin and Microtubules Differently Contribute to Vacuolar Targeting Specificity during the Export from the ER

et al. 2021

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“…Arabidopsis has 19 ARFs and ARLs, and with few exceptions, most remain uncharacterized (Delgadillo et al, 2020;Gebbie et al, 2005;McElver et al, 2000;Vernoud et al, 2003;Xu and Scheres, 2005). The roles attributed to members of this familye.g.…”

Section: Discussionmentioning

confidence: 99%

Members of the ELMOD protein family specify formation of distinct aperture domains on the Arabidopsis pollen surface

Zhou

Amom

Reeder

et al. 2021

Preprint

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Pollen apertures, the characteristic gaps in pollen wall exine, have emerged as a model for studying the formation of distinct plasma-membrane domains. In each species, aperture number, position, and morphology are typically fixed; across species they vary widely. During pollen development certain plasma-membrane domains attract specific proteins and lipids and become protected from exine deposition, developing into apertures. However, how these aperture domains are selected is unknown. Here, we demonstrate that patterns of aperture domains in Arabidopsis are controlled by the members of the ancient ELMOD protein family, which, although important in animals, has not been studied in plants. We show that two members of this family, MACARON (MCR) and ELMOD_A, act upstream of the previously discovered aperture proteins and that their expression levels influence the number of aperture domains that form on the surface of developing pollen grains. We also show that a third ELMOD family member, ELMOD_E, can interfere with MCR and ELMOD_A activities, changing aperture morphology and producing new aperture patterns. Our findings reveal key players controlling early steps in aperture domain formation, identify residues important for their function, and open new avenues for investigating how diversity of aperture patterns in nature is achieved.

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“…Cytoplasmic streaming, the myosin-driven directional flow of the cytoplasm, also plays a role in plant cell ER dynamics [ 237 , 238 ]. Interestingly, a novel ER and microtubule-associated compartment (EMAC) has been identified in plants that is anchored on microtubules, thereby resisting this flow [ 239 ]. Similarly, stable tubular ER junctions have also been observed to associate with microtubules [ 240 ].…”

Section: Er Dynamicsmentioning

confidence: 99%

Intertwined and Finely Balanced: Endoplasmic Reticulum Morphology, Dynamics, Function, and Diseases

Perkins

Allan

2021

Cells

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The endoplasmic reticulum (ER) is an organelle that is responsible for many essential subcellular processes. Interconnected narrow tubules at the periphery and thicker sheet-like regions in the perinuclear region are linked to the nuclear envelope. It is becoming apparent that the complex morphology and dynamics of the ER are linked to its function. Mutations in the proteins involved in regulating ER structure and movement are implicated in many diseases including neurodegenerative diseases such as Alzheimer’s, Parkinson’s, and amyotrophic lateral sclerosis (ALS). The ER is also hijacked by pathogens to promote their replication. Bacteria such as Legionella pneumophila and Chlamydia trachomatis, as well as the Zika virus, bind to ER morphology and dynamics-regulating proteins to exploit the functions of the ER to their advantage. This review covers our understanding of ER morphology, including the functional subdomains and membrane contact sites that the organelle forms. We also focus on ER dynamics and the current efforts to quantify ER motion and discuss the diseases related to ER morphology and dynamics.

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MTV proteins unveil ER- and microtubule-associated compartments in the plant vacuolar trafficking pathway

Cited by 25 publications

References 89 publications

Actin and Microtubules Differently Contribute to Vacuolar Targeting Specificity during the Export from the ER

Actin and Microtubules Differently Contribute to Vacuolar Targeting Specificity during the Export from the ER

Members of the ELMOD protein family specify formation of distinct aperture domains on the Arabidopsis pollen surface

Intertwined and Finely Balanced: Endoplasmic Reticulum Morphology, Dynamics, Function, and Diseases

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