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Yao, Tso-Pang

Masahide Fukada, Atsuo Nakayama, Takayoshi Mamiya, Tso-Pang Yao, Yoshiharu Kawaguchi
Histone deacetylase 6 (Hdac6), a multifunctional cytoplasmic deacetylase, is abundant in brain. We previously demonstrated that global Hdac6 depletion causes aberrant emotional behaviors in mice. Identification of affected brain systems and its molecular basis will lead to new insights into relations between protein acetylation events and psychiatric disorders. Here we report the dopaminergic abnormalities in Hdac6 KO mice. The dopamine transmission mediated by D1-like and D2-like G protein-coupled dopamine receptors is known to play roles in controlling movement, cognition, and motivational processes, and its dysfunction causes psychiatric disorders...
November 2016: Neuropharmacology
Norman Núñez-Andrade, Salvador Iborra, Antonio Trullo, Olga Moreno-Gonzalo, Enrique Calvo, Elena Catalán, Gaël Menasche, David Sancho, Jesús Vázquez, Tso-Pang Yao, Noa Beatriz Martín-Cófreces, Francisco Sánchez-Madrid
HDAC6 is a tubulin deacetylase involved in many cellular functions related to cytoskeleton dynamics, including cell migration and autophagy. In addition, HDAC6 affects antigen-dependent CD4(+)T cell activation. In this study, we show that HDAC6 contributes to the cytotoxic function of CD8(+)T cells. Immunization studies revealed defective cytotoxic activity in vivo in the absence of HDAC6. Adoptive transfer of wild-type or Hdac6(-/-)CD8(+)T cells to Rag1(-/-)mice demonstrated specific impairment in CD8(+)T cell responses against vaccinia infection...
April 1, 2016: Journal of Cell Science
Shuchen Gu, Yanjing Liu, Bowen Zhu, Ke Ding, Tso-Pang Yao, Fenfang Chen, Lixing Zhan, Pinglong Xu, Marcelo Ehrlich, Tingbo Liang, Xia Lin, Xin-Hua Feng
The epithelial-to-mesenchymal transition (EMT) is a process by which differentiated epithelial cells reprogram gene expression, lose their junctions and polarity, reorganize their cytoskeleton, increase cell motility and assume a mesenchymal morphology. Despite the critical functions of the microtubule (MT) in cytoskeletal organization, how it participates in EMT induction and maintenance remains poorly understood. Here we report that acetylated α-tubulin, which plays an important role in microtubule (MT) stabilization and cell morphology, can serve as a novel regulator and marker of EMT...
March 4, 2016: Journal of Biological Chemistry
Su Jin Choi, Hyun-Cheol Lee, Jae-Hoon Kim, Song Yi Park, Tae-Hwan Kim, Woon-Kyu Lee, Duk-Jae Jang, Ji-Eun Yoon, Young-Il Choi, Seihwan Kim, JinYeul Ma, Chul-Joong Kim, Tso-Pang Yao, Jae U Jung, Joo-Yong Lee, Jong-Soo Lee
RIG-I is a key cytosolic sensor that detects RNA viruses through its C-terminal region and activates the production of antiviral interferons (IFNs) and proinflammatory cytokines. While posttranslational modification has been demonstrated to regulate RIG-I signaling activity, its significance for the sensing of viral RNAs remains unclear. Here, we first show that the RIG-I C-terminal region undergoes deacetylation to regulate its viral RNA-sensing activity and that the HDAC6-mediated deacetylation of RIG-I is critical for viral RNA detection...
February 15, 2016: EMBO Journal
Joo-Yong Lee, Yoshiharu Kawaguchi, Ming Li, Meghan Kapur, Su Jin Choi, Hak-June Kim, Song-Yi Park, Haining Zhu, Tso-Pang Yao
Aberrant accumulation of protein aggregates is a pathological hallmark of many neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS). Although a buildup of protein aggregates frequently leads to cell death, whether it is the key pathogenic factor in driving neurodegenerative disease remains controversial. HDAC6, a cytosolic ubiquitin-binding deacetylase, has emerged as an important regulator of ubiquitin-dependent quality control autophagy, a lysosome-dependent degradative system responsible for the disposal of misfolded protein aggregates and damaged organelles...
2015: Neuro-degenerative Diseases
Hak-June Kim, Yoshito Nagano, Su Jin Choi, Song Yi Park, Hongtae Kim, Tso-Pang Yao, Joo-Yong Lee
Mitochondria undergo fusion and fission in response to various metabolic stresses. Growing evidences have suggested that the morphological change of mitochondria by fusion and fission plays a critical role in protecting mitochondria from metabolic stresses. Here, we showed that hypoxia treatment could induce interaction between HDAC6 and MFN2, thus protecting mitochondrial connectivity. Mechanistically, we demonstrated that a mitochondrial ubiquitin ligase MARCH5/MITOL was responsible for hypoxia-induced MFN2 degradation in HDAC6 deficient cells...
September 4, 2015: Biochemical and Biophysical Research Communications
Kristi L Norris, Rui Hao, Liang-Fu Chen, Chun-Hsiang Lai, Meghan Kapur, Peter J Shaughnessy, Dennis Chou, Jin Yan, J Paul Taylor, Simone Engelender, Anna E West, Kah-Leong Lim, Tso-Pang Yao
Mutations in PARKIN (PARK2), an ubiquitin ligase, cause early onset Parkinson disease. Parkin was shown to bind, ubiquitinate, and target depolarized mitochondria for destruction by autophagy. This process, mitophagy, is considered crucial for maintaining mitochondrial integrity and suppressing Parkinsonism. Here, we report that under moderate mitochondrial stress, parkin does not translocate to mitochondria to induce mitophagy; rather, it stimulates mitochondrial connectivity. Mitochondrial stress-induced fusion requires PINK1 (PARK6), mitofusins, and parkin ubiquitin ligase activity...
May 29, 2015: Journal of Biological Chemistry
Todd J Cohen, Moon-Chang Choi, Meghan Kapur, Vitor A Lira, Zhen Yan, Tso-Pang Yao
Fiber type-specific programs controlled by the transcription factor MEF2 dictate muscle functionality. Here, we show that HDAC4, a potent MEF2 inhibitor, is predominantly localized to the nuclei in fast/glycolytic fibers in contrast to the sarcoplasm in slow/oxidative fibers. The cytoplasmic localization is associated with HDAC4 hyper-phosphorylation in slow/oxidative-fibers. Genetic reprogramming of fast/glycolytic fibers to oxidative fibers by active CaMKII or calcineurin leads to increased HDAC4 phosphorylation, HDAC4 nuclear export, and an increase in markers associated with oxidative fibers...
April 2015: Molecules and Cells
Priyaanka Nanduri, Rui Hao, Thomas Fitzpatrick, Tso-Pang Yao
Efficient elimination of misfolded proteins by the proteasome system is critical for proteostasis. Inadequate proteasome capacity can lead to aberrant aggregation of misfolded proteins and inclusion body formation, a hallmark of neurodegenerative disease. The proteasome system cannot degrade aggregated proteins; however, it stimulates autophagy-dependent aggregate clearance by producing unanchored lysine (K)63-linked ubiquitin chains via the proteasomal deubiquitinating enzyme Poh1. The canonical function of Poh1, which removes ubiquitin chains en bloc from proteasomal substrates prior to their degradation, requires intact 26S proteasomes...
April 10, 2015: Journal of Biological Chemistry
Yanhua Rao, Rui Hao, Bin Wang, Tso-Pang Yao
Primary cilia are specialized, acetylated microtubule-based signaling processes. Cilium assembly is activated by cellular quiescence and requires reconfiguration of microtubules, the actin cytoskeleton, and vesicular trafficking machinery. How these components are coordinated to activate ciliogenesis remains unknown. Here we identify the microtubule acetyltransferase Mec-17 and myosin II motors as the key effectors in primary cilium biogenesis. We found that myosin IIB (Myh10) is required for cilium formation; however, myosin IIA (Myh9) suppresses it...
2014: PloS One
Linlin Zhang, Shanshan Liu, Ningning Liu, Yong Zhang, Min Liu, Dengwen Li, Edward Seto, Tso-Pang Yao, Wenqing Shui, Jun Zhou
Histone deacetylase 6 (HDAC6), a predominantly cytoplasmic protein deacetylase, participates in a wide range of cellular processes through its deacetylase activity. However, the diverse functions of HDAC6 cannot be fully elucidated with its known substrates. In an attempt to explore the substrate diversity of HDAC6, we performed quantitative proteomic analyses to monitor changes in the abundance of protein lysine acetylation in response to HDAC6 deficiency. We identified 107 proteins with elevated acetylation in the liver of HDAC6 knockout mice...
January 2015: Protein & Cell
Joo-Yong Lee, Meghan Kapur, Ming Li, Moon-Chang Choi, Sujin Choi, Hak-June Kim, Inhye Kim, Eunji Lee, J Paul Taylor, Tso-Pang Yao
Fasting and glucose shortage activate a metabolic switch that shifts more energy production to mitochondria. This metabolic adaptation ensures energy supply, but also elevates the risk of mitochondrial oxidative damage. Here, we present evidence that metabolically challenged mitochondria undergo active fusion to suppress oxidative stress. In response to glucose starvation, mitofusin 1 (MFN1) becomes associated with the protein deacetylase HDAC6. This interaction leads to MFN1 deacetylation and activation, promoting mitochondrial fusion...
November 15, 2014: Journal of Cell Science
Moon-Chang Choi, Soyoung Ryu, Rui Hao, Bin Wang, Meghan Kapur, Chen-Ming Fan, Tso-Pang Yao
During muscle regeneration, the transcription factor Pax7 stimulates the differentiation of satellite cells (SCs) toward the muscle lineage but restricts adipogenesis. Here, we identify HDAC4 as a regulator of Pax7-dependent muscle regeneration. In HDAC4-deficient SCs, the expression of Pax7 and its target genes is reduced. We identify HDAC4-regulated Lix1 as a Pax7 target gene required for SC proliferation. HDAC4 inactivation leads to defective SC proliferation, muscle regeneration, and aberrant lipid accumulation...
November 2014: EMBO Reports
Bin Wang, Ting-Yu Liu, Chun-Hsiang Lai, Yan-hua Rao, Moon-Chang Choi, Jen-Tsan Chi, Jian-wu Dai, Jeffrey C Rathmell, Tso-Pang Yao
Activation of the inflammatory response is accompanied by a metabolic shift to aerobic glycolysis. Here we identify histone deacetylase 4 (HDAC4) as a new component of the immunometabolic program. We show that HDAC4 is required for efficient inflammatory cytokine production activated by lipopolysaccharide (LPS). Surprisingly, prolonged LPS treatment leads to HDAC4 degradation. LPS-induced HDAC4 degradation requires active glycolysis controlled by GSK3β and inducible nitric oxide synthase (iNOS). Inhibition of GSK3β or iNOS suppresses nitric oxide (NO) production, glycolysis, and HDAC4 degradation...
November 1, 2014: Molecular Biology of the Cell
Bin Wang, Yan-Hua Rao, Makoto Inoue, Rui Hao, Chun-Hsiang Lai, David Chen, Stacey L McDonald, Moon-Chang Choi, Qiu Wang, Mari L Shinohara, Tso-Pang Yao
Reversible acetylation of α-tubulin is an evolutionarily conserved modification in microtubule networks. Despite its prevalence, the physiological function and regulation of microtubule acetylation remain poorly understood. Here we report that macrophages challenged by bacterial lipopolysaccharides (LPS) undergo extensive microtubule acetylation. Suppression of LPS-induced microtubule acetylation by inactivating the tubulin acetyltransferase, MEC17, profoundly inhibits the induction of anti-inflammatory interleukin-10 (IL-10), a phenotype effectively reversed by an acetylation-mimicking α-tubulin mutant...
2014: Nature Communications
Rui Hao, Priyaanka Nanduri, Yanhua Rao, R Scott Panichelli, Akihiro Ito, Minoru Yoshida, Tso-Pang Yao
Aberrant protein aggregation is a dominant pathological feature in neurodegenerative diseases. Protein aggregates cannot be processed by the proteasome; instead, they are frequently concentrated to the aggresome, a perinuclear inclusion body, and subsequently removed by autophagy. Paradoxically, proteasomes are also concentrated at aggresomes and other related inclusion bodies prevalent in neurodegenerative disease. Here, we show that proteasomes are crucial components in aggresome clearance. The disassembly and disposal of aggresomes requires Poh1, a proteasomal deubiquitinating enzyme that cleaves ubiquitinated proteins and releases ubiquitin chains...
September 26, 2013: Molecular Cell
Nam Chul Kim, Emilie Tresse, Regina-Maria Kolaitis, Amandine Molliex, Ruth E Thomas, Nael H Alami, Bo Wang, Aashish Joshi, Rebecca B Smith, Gillian P Ritson, Brett J Winborn, Jennifer Moore, Joo-Yong Lee, Tso-Pang Yao, Leo Pallanck, Mondira Kundu, J Paul Taylor
Mutations in VCP cause multisystem degeneration impacting the nervous system, muscle, and/or bone. Patients may present with ALS, Parkinsonism, frontotemporal dementia, myopathy, Paget's disease, or a combination of these. The disease mechanism is unknown. We developed a Drosophila model of VCP mutation-dependent degeneration. The phenotype is reminiscent of PINK1 and parkin mutants, including a pronounced mitochondrial defect. Indeed, VCP interacts genetically with the PINK1/parkin pathway in vivo. Paradoxically, VCP complements PINK1 deficiency but not parkin deficiency...
April 10, 2013: Neuron
Kristi L Norris, Tso-Pang Yao
Nutrient deprivation or cellular stress leads to the activation of a catabolic pathway that is conserved across species, known as autophagy. This process is considered to be adaptive and plays an important role in a number of cellular processes, including metabolism, immunity and development. Autophagy has also been linked to diseases, such as cancer and neurodegeneration, highlighting the importance of a better insight into its regulation. In the present chapter, we discuss how PTMs (post-translational modifications) of lysine residues by acetylation and ubiquitination alter the function of key proteins involved in the activation, maturation and substrate selectivity of autophagy...
2012: Essays in Biochemistry
Moon-Chang Choi, Todd J Cohen, Tomasa Barrientos, Bin Wang, Ming Li, Bryan J Simmons, Jeong Soo Yang, Gregory A Cox, Yingming Zhao, Tso-Pang Yao
Prolonged deficits in neural input activate pathological muscle remodeling, leading to atrophy. In denervated muscle, activation of the atrophy program requires HDAC4, a potent repressor of the master muscle transcription factor MEF2. However, the signaling mechanism that connects HDAC4, a protein deacetylase, to the atrophy machinery remains unknown. Here, we identify the AP1 transcription factor as a critical target of HDAC4 in neurogenic muscle atrophy. In denervated muscle, HDAC4 activates AP1-dependent transcription, whereas AP1 inactivation recapitulates HDAC4 deficiency and blunts the muscle atrophy program...
July 13, 2012: Molecular Cell
Masahide Fukada, Atsuko Hanai, Atsuo Nakayama, Takayoshi Suzuki, Naoki Miyata, Ramona M Rodriguiz, William C Wetsel, Tso-Pang Yao, Yoshiharu Kawaguchi
Acetylation is mediated by acetyltransferases and deacetylases, and occurs not only on histones but also on diverse proteins. Although histone acetylation in chromatin structure and transcription has been well studied, the biological roles of non-histone acetylation remain elusive. Histone deacetylase 6 (Hdac6), a member of the histone deacetylase (HDAC) family, is a unique deacetylase that localizes to cytoplasm and functions in many cellular events by deacetylating non-histone proteins including α-tubulin, Hsp90, and cortactin...
2012: PloS One
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