Formins: Emerging Players in the Dynamic Plant Cell Cortex

Cvrčková, Fatima

doi:10.6064/2012/712605

Cited by 7 publications

(8 citation statements)

References 176 publications

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“…Plant formin homologs are quite different in structure and function [ 54 ]. Plant formins may play important roles in cell cortex organization, including cortical actin, microtubule cytoskeletons, and the attachment to the plasma membrane [ 55 ]. In this study, formin homolog EXTs (FH EXTs) were categorized as a third group of chimeric EXTs, as some of the formin homologs were found to have an N terminal signal peptide and contain a number of SP n repeats.…”

Section: Resultsmentioning

confidence: 99%

Bioinformatic Identification and Analysis of Extensins in the Plant Kingdom

et al. 2016

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Extensins (EXTs) are a family of plant cell wall hydroxyproline-rich glycoproteins (HRGPs) that are implicated to play important roles in plant growth, development, and defense. Structurally, EXTs are characterized by the repeated occurrence of serine (Ser) followed by three to five prolines (Pro) residues, which are hydroxylated as hydroxyproline (Hyp) and glycosylated. Some EXTs have Tyrosine (Tyr)-X-Tyr (where X can be any amino acid) motifs that are responsible for intramolecular or intermolecular cross-linkings. EXTs can be divided into several classes: classical EXTs, short EXTs, leucine-rich repeat extensins (LRXs), proline-rich extensin-like receptor kinases (PERKs), formin-homolog EXTs (FH EXTs), chimeric EXTs, and long chimeric EXTs. To guide future research on the EXTs and understand evolutionary history of EXTs in the plant kingdom, a bioinformatics study was conducted to identify and classify EXTs from 16 fully sequenced plant genomes, including Ostreococcus lucimarinus, Chlamydomonas reinhardtii, Volvox carteri, Klebsormidium flaccidum, Physcomitrella patens, Selaginella moellendorffii, Pinus taeda, Picea abies, Brachypodium distachyon, Zea mays, Oryza sativa, Glycine max, Medicago truncatula, Brassica rapa, Solanum lycopersicum, and Solanum tuberosum, to supplement data previously obtained from Arabidopsis thaliana and Populus trichocarpa. A total of 758 EXTs were newly identified, including 87 classical EXTs, 97 short EXTs, 61 LRXs, 75 PERKs, 54 FH EXTs, 38 long chimeric EXTs, and 346 other chimeric EXTs. Several notable findings were made: (1) classical EXTs were likely derived after the terrestrialization of plants; (2) LRXs, PERKs, and FHs were derived earlier than classical EXTs; (3) monocots have few classical EXTs; (4) Eudicots have the greatest number of classical EXTs and Tyr-X-Tyr cross-linking motifs are predominantly in classical EXTs; (5) green algae have no classical EXTs but have a number of long chimeric EXTs that are absent in embryophytes. Furthermore, phylogenetic analysis was conducted of LRXs, PERKs and FH EXTs, which shed light on the evolution of three EXT classes.

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Section: Resultsmentioning

confidence: 99%

Bioinformatic Identification and Analysis of Extensins in the Plant Kingdom

et al. 2016

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“…Surprisingly, FH2-mediated formin heterodimerization has been neither documented nor excluded yet in any organism, albeit dimerization via other domains was reported (see Cvrvčková, 2012). …”

Section: Membrane-associated Formins In Plants: the Known And The Posmentioning

confidence: 99%

“…Here studies in plants have led the way, with typical Class I formins predicted and later experimentally proven to be directly inserted into membranes, especially the plasmalemma (Banno and Chua, 2000; Cvrvčková, 2000; further experimental evidence reviewed below and in Cvrvčková, 2012 and van Gisbergen and Bezanilla, 2013). Also Class II formins often possess a domain related to metazoan phosphoinositide phosphatase PTEN, which may mediate their peripheral association with membranes (Cvrvčková et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Formins and membranes: anchoring cortical actin to the cell wall and beyond

Cvrčková

2013

Front. Plant Sci.

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Formins are evolutionarily conserved eukaryotic proteins participating in actin and microtubule organization. Land plants have three formin clades, with only two – Class I and II – present in angiosperms. Class I formins are often transmembrane proteins, residing at the plasmalemma and anchoring the cortical cytoskeleton across the membrane to the cell wall, while Class II formins possess a PTEN-related membrane-binding domain. Lower plant Class III and non-plant formins usually contain domains predicted to bind RHO GTPases that are membrane-associated. Thus, some kind of membrane anchorage appears to be a common formin feature. Direct interactions between various non-plant formins and integral or peripheral membrane proteins have indeed been reported, with varying mechanisms and biological implications. Besides of summarizing new data on Class I and Class II formin-membrane relationships, this review surveys such “non-classical” formin-membrane interactions and examines which, if any, of them may be evolutionarily conserved and operating also in plants. FYVE, SH3 and BAR domain-containing proteins emerge as possible candidates for such conserved membrane-associated formin partners.

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“…OsFH5 (also named RMD and BUI1) belongs to type II formin in plant, contains one PTEN (phosphatase and tensin homolog), one FH1 and one FH2 domain (Zhang et al, Yang et al), previous study showed that the mutants showed severe de ciency in most tissues of rice, such as, waved roots, dwarf lines, aberrant seeds shape, stronger sensitivity to gravity (Zhang et al, Huang et al, Song et al, 2019). PTEN domain of formins play important role in attaching with membrane, for instance, plasma membrane and chloroplast, mitochondrion, endoplasmic reticulum and so on (van Gisbergen and Bezanilla, Cvrckova, 2012, Cvrcková, 2013, while FH (formin homology domain)1 is used for binding pro lin/actin complex, FH2 is essential for nuclear activity (Cao et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

RIPs Interact with OsFH5 and Control the Rice Morphology by Affecting Stability of OsFH5

Chang

Yang

Liang

et al. 2021

Preprint

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E3 ubiquitin ligases have been more widely reported to mediate the degradation of target proteins. In our research, one SIAH type E3 ligase was identified, named RIP1, and there are five genes were found to be highly homologous to it, named RIP2 to RIP6 dividedly. Y2H and BiFC were carried out to prove the interaction between RIPs and OsFH5, moreover, homo- and hetero- oligomers can be formed among RIPs and they all can affect the localization of OsFH5. Degradation experiments showed that RIP1 is able to slow down the degradation rate of OsFH5, and also RIP5, RIP6. There was no obvious phenotype in both RIP1 overexpression and mutant transgenic lines, whereas in rips multi-knock out lines showed up similar defects to osfh5, such as, dwarf height; less smooth and rounder seeds; leaves width became wilder. Otherwise, rips also exhibit some special phenotypes, for instance, the angles between leaves and stems were appreciable enlarged; spiral crimped roots. In addition, microfilaments organization in rips appeared disordered than wild type. All above illustrate that RIPs influence morphology by interacting with OsFH5 and affecting its subcellular localization, stability or maybe involved in other pathways in rice.

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Formins: Emerging Players in the Dynamic Plant Cell Cortex

Cited by 7 publications

References 176 publications

Bioinformatic Identification and Analysis of Extensins in the Plant Kingdom

Bioinformatic Identification and Analysis of Extensins in the Plant Kingdom

Formins and membranes: anchoring cortical actin to the cell wall and beyond

RIPs Interact with OsFH5 and Control the Rice Morphology by Affecting Stability of OsFH5

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