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Paul J. Park,Fthimnir M. Hassan,Xavier E. Ferrer,Cole Morrissette,Nathan J. Lee,Meghan Cerpa,Zeeshan M. Sardar,Michael P. Kelly,Stephane Bourret,Kazuhiro Hasegawa,Hee-Kit Wong,Gabriel Liu,Hwee Weng De 대한척추신경외과학회 2023 Neurospine Vol.20 No.3
Objective: To define a novel radiographic measurement, the posterior cranial vertical line (PCVL), in an asymptomatic adult population to better understand global sagittal alignment. Methods: We performed a multicenter retrospective review of prospectively collected radiographic data on asymptomatic volunteers aged 20–79. The PCVL is a vertical plumb line drawn from the posterior-most aspect of the occiput. The horizontal distances of the PCVL to the thoracic apex (TA), posterior sagittal vertical line (PSVL, posterosuperior endplate of S1), femoral head center, and tibial plafond were measured. Classification was either grade 1 (PCVL posterior to TA and PSVL), grade 2 (PCVL anterior to TA and posterior to PSVL), or grade 3 (PCVL anterior to TA and PSVL). Results: Three hundred thirty-four asymptomatic patients were evaluated with a mean age of 41 years. Eighty-three percent of subjects were PCVL grade 1, 15% were grade 2, and 3% were grade 3. Increasing PCVL grade was associated with increased age (p < 0.001), C7–S1 sagittal vertical axis (SVA) (p < 0.001), C2–7 SVA (p < 0.001). Additionally, it was associated with decreased SS (p = 0.045), increased PT (p < 0.001), and increased knee flexion (p < 0.001). Conclusion: The PCVL is a radiographic marker of global sagittal alignment that is simple to implement and interpret. Increasing PCVL grade was significantly associated with expected changes and compensatory mechanisms in the aging population. Most importantly, it incorporates cervical alignment parameters such as C2–7 SVA. The PCVL defines global sagittal alignment in adult volunteers and naturally distributes into 3 grades, with only 3% being grade 3 where the PCVL lies anterior to the TA and PSVL.
Narasimhan, Meena L.,Coca, Maria A.,Jin, Jingbo,Yamauchi, Toshimasa,Ito, Yusuke,Kadowaki, Takashi,Kim, Kyeong-Kyu,Pardo, Jose M,Damsz, Barbara,Hasegawa, Paul M.,Yun, Dae-Jin,Bressan, Ray A. Plant molecular biology and biotechnology research 2005 Plant molecular biology and biotechnology research Vol.2005 No.
The antifungal activity of the PR-5 family of plant defense proteins has been suspected to involve specific plasma membrane component(s) of the fungal target. Osmotin is a tobacco PR-5 family protein that induces apoptosis in the yeast Saccharomyces cerevisiae. We show here that the protein encoded by ORE20/PHO36(YOL002c), a seven transmembrane domain receptor-like polypeptide that regulates lipid and phosphate metabolism, is an osmotin binding plasma mrmbrane protein that is required for full sensitivity to osmotin. PHO36 functions upstream of RAS2 in the osmotin-induced apoptotic pathway. The mammalian homolog of PHO36 is a receptor for the hormone adiponectin and regulates cellular lipid and sugar metabolism. OS-motion and adiponectin, the corresponding "receptor" binding proteins, do not share sequence similarity. However, the β barrel domain of both proteins can be overlapped, and osmotin, like adiponectin, activates AMP kinase in C2C12 myocytes via adiponectin receptors.
Involvement of Arabidopsis HOS15 in histone deacetylation and cold tolerance.
Zhu, Jianhua,Jeong, Jae Cheol,Zhu, Yanmei,Sokolchik, Irina,Miyazaki, Saori,Zhu, Jian-Kang,Hasegawa, Paul M,Bohnert, Hans J,Shi, Huazhong,Yun, Dae-Jin,Bressan, Ray A National Academy of Sciences 2008 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.105 No.12
<P>Histone modification in chromatin is one of the key control points in gene regulation in eukaryotic cells. Protein complexes composed of histone acetyltransferase or deacetylase, WD40 repeat protein, and many other components have been implicated in this process. Here, we report the identification and functional characterization of HOS15, a WD40-repeat protein crucial for repression of genes associated with abiotic stress tolerance through histone deacetylation in Arabidopsis. HOS15 shares high sequence similarity with human transducin-beta like protein (TBL), a component of a repressor protein complex involved in histone deacetylation. Mutation of the HOS15 gene renders mutant plants hypersensitive to freezing temperatures. HOS15 is localized in the nucleus and specifically interacts with histone H4. The level of acetylated histone H4 is higher in the hos15 mutant than in WT plants. Moreover, the stress inducible RD29A promoter is hyperinduced and associated with a substantially higher level of acetylated histone H4 in the hos15 mutant under cold stress conditions. Our results suggest a critical role for gene activation/repression by histone acetylation/deacetylation in plant acclimation and tolerance to cold stress.</P>
Bang, Wooyoung,Kim, Sewon,Ueda, Akihiro,Vikram, Meenu,Yun, Daejin,Bressan, Ray A,Hasegawa, Paul M,Bahk, Jeongdong,Koiwa, Hisashi American Society of Plant Physiologists 2006 Plant Physiology Vol.142 No.2
<P>An Arabidopsis (Arabidopsis thaliana) multigene family (predicted to be more than 20 members) encodes plant C-terminal domain (CTD) phosphatases that dephosphorylate Ser residues in tandem heptad repeat sequences of the RNA polymerase II C terminus. CTD phosphatase-like (CPL) isoforms 1 and 3 are regulators of osmotic stress and abscisic acid (ABA) signaling. Evidence presented herein indicates that CPL3 and CPL4 are homologs of a prototype CTD phosphatase, FCP1 (TFIIF-interacting CTD-phosphatase). CPL3 and CPL4 contain catalytic FCP1 homology and breast cancer 1 C terminus (BRCT) domains. Recombinant CPL3 and CPL4 interact with AtRAP74, an Arabidopsis ortholog of a FCP1-interacting TFIIF subunit. A CPL3 or CPL4 C-terminal fragment that contains the BRCT domain mediates molecular interaction with AtRAP74. Consistent with their predicted roles in transcriptional regulation, green fluorescent protein fusion proteins of CPL3, CPL4, and RAP74 all localize to the nucleus. cpl3 mutations that eliminate the BRCT or FCP1 homology domain cause ABA hyperactivation of the stress-inducible RD29a promoter, whereas RNAi suppression of CPL4 results in dwarfism and reduced seedling growth. These results indicate CPL3 and CPL4 are a paralogous pair of general transcription regulators with similar biochemical properties, but are required for the distinct developmental and environmental responses. CPL4 is necessary for normal plant growth and thus most orthologous to fungal and metazoan FCP1, whereas CPL3 is an isoform that specifically facilitates ABA signaling.</P>
Hisashi Koiwa,,Stephane Hausmann,Bang, Woo-Young,Akihiro Ueda,Naoko Kondo,Akihiro Hiraguri,Toshiyuki Fuku,hara,Bahk, Jeong-Dong,Yun, Dae-Jin,Ray A. Bressan,Paul M. Hasegawa,Stewart Shuman Plant molecular biology and biotechnology research 2004 Plant molecular biology and biotechnology research Vol.2004 No.-
Transcription and mRNA processing are regulated by phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase Ⅱ, which consists of tandem repeats of a Y^(1)S^(2)P^(3)T^(4)S^(5)P^(6)S^(7) heptapeptide. Previous studies showed that members of the plant CTD phosphatase-like (CPL) protein family differentially regulate osmotic stress-responsive and abscisic acid-responsive transcription in Arabidopsis thaliana. Here we report that AtCPL1 and AtCPL2 specifically dephosphorylate Ser-5 of the CTD heptad in Arabidopsis RNA polymerase Ⅱ, but not Ser-2. An N-terminal catalytic domain of CPL1, which suffices for CTD Ser-5 phosphatase activity in virto, includes a signature DXDXT acylphosphatase motif, but lacks a breast cancer 1 CTD, which is an essential component of the fungal and metazoan Fcp1 CTD phosphatase enzymes. The CTD of CPL1, which contains two putative double-stranded RNA binding motifs, is essential for the in vivo function of CPL1 and includes a C-terminal 23-aa signal responsible for its nuclear targeting. CPL2 has a similar domain structure but contains only one double-stranded RNA binding motif. Combining mutant alleles of CPL1 and CPL2 causes synthetic lethality of the male but not the female gametes. These results indicate that CPL1 and CPL2 exemplify a unique family of CTD Ser-5-specific phosphatases with an essential role in plant growth and development.
Miura, Kenji,Jin, Jing Bo,Lee, Jiyoung,Yoo, Chan Yul,Stirm, Vicki,Miura, Tomoko,Ashworth, Edward N,Bressan, Ray A,Yun, Dae-Jin,Hasegawa, Paul M Americ 2007 The Plant cell Vol.19 No.4
<P>SIZ1 is a SUMO E3 ligase that facilitates conjugation of SUMO to protein substrates. siz1-2 and siz1-3 T-DNA insertion alleles that caused freezing and chilling sensitivities were complemented genetically by expressing SIZ1, indicating that the SIZ1 is a controller of low temperature adaptation in plants. Cold-induced expression of CBF/DREB1, particularly of CBF3/DREB1A, and of the regulon genes was repressed by siz1. siz1 did not affect expression of ICE1, which encodes a MYC transcription factor that is a controller of CBF3/DREB1A. A K393R substitution in ICE1 [ICE1(K393R)] blocked SIZ1-mediated sumoylation in vitro and in protoplasts identifying the K393 residue as the principal site of SUMO conjugation. SIZ1-dependent sumoylation of ICE1 in protoplasts was moderately induced by cold. Sumoylation of recombinant ICE1 reduced polyubiquitination of the protein in vitro. ICE1(K393R) expression in wild-type plants repressed cold-induced CBF3/DREB1A expression and increased freezing sensitivity. Furthermore, expression of ICE1(K393R) induced transcript accumulation of MYB15, which encodes a MYB transcription factor that is a negative regulator of CBF/DREB1. SIZ1-dependent sumoylation of ICE1 may activate and/or stabilize the protein, facilitating expression of CBF3/DREB1A and repression of MYB15, leading to low temperature tolerance.</P>
Zhu, Jianhua,Fu, Xinmiao,Koo, Yoon Duck,Zhu, Jian-Kang,Jenney Jr., Francis E.,Adams, Michael W. W.,Zhu, Yanmei,Shi, Huazhong,Yun, Dae-Jin,Hasegawa, Paul M.,Bressan, Ray A. American Society for Microbiology 2007 Molecular and cellular biology Vol.27 No.14
<B>ABSTRACT</B><P>The myristoylated calcium sensor SOS3 and its interacting protein kinase, SOS2, play critical regulatory roles in salt tolerance. Mutations in either of these proteins render <I>Arabidopsis thaliana</I> plants hypersensitive to salt stress. We report here the isolation and characterization of a mutant called <I>enh1-1</I> that enhances the salt sensitivity of <I>sos3-1</I> and also causes increased salt sensitivity by itself. <I>ENH1</I> encodes a chloroplast-localized protein with a PDZ domain at the N-terminal region and a rubredoxin domain in the C-terminal part. Rubredoxins are known to be involved in the reduction of superoxide in some anaerobic bacteria. The <I>enh1-1</I> mutation causes enhanced accumulation of reactive oxygen species (ROS), particularly under salt stress. ROS also accumulate to higher levels in <I>sos2-1</I> but not in <I>sos3-1</I> mutants. The <I>enh1-1</I> mutation does not enhance <I>sos2-1</I> phenotypes. Also, <I>enh1-1</I> and <I>sos2-1</I> mutants, but not <I>sos3-1</I> mutants, show increased sensitivity to oxidative stress. These results indicate that ENH1 functions in the detoxification of reactive oxygen species resulting from salt stress by participating in a new salt tolerance pathway that may involve SOS2 but not SOS3.</P>