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Your search keyword '"Geisbrecht, Erika R."' showing total 143 results
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143 results on '"Geisbrecht, Erika R."'

2. Skeletal Muscle Metabolism Is Dynamic during Porcine Postnatal Growth.

Author

Rimmer, Linnea A., Geisbrecht, Erika R., Chao, Michael D., O'Quinn, Travis G., Woodworth, Jason C., and Zumbaugh, Morgan D.

Subjects
MUSCLE metabolism, METABOLOMIC fingerprinting, SKELETAL muscle, SWINE nutrition, PYRUVATE carboxylase, LATISSIMUS dorsi (Muscles)
Abstract

Skeletal muscle metabolism has implications for swine feed efficiency (FE); however, it remains unclear if the metabolic profile of skeletal muscle changes during postnatal growth. To assess the metabolic changes, samples were collected from the longissimus dorsi (LD, glycolytic muscle), latissimus dorsi (LAT, mixed muscle), and masseter (MS, oxidative muscle) at 20, 53, 87, 120, and 180 days of age from barrows. Muscles were assessed to determine the abundance of several metabolic enzymes. Lactate dehydrogenase (LDHα) decreased in all muscles from 20 to 87 d (p < 0.01), which may be attributed to the muscles being more glycolytic at weaning from a milk-based diet. Pyruvate carboxylase (PC) increased in all muscles at 53 d compared to the other time points (p < 0.01), while pyruvate dehydrogenase α 1 (PDHα1) increased at 87 and 180 d in MS compared to LD (p < 0.05), indicating that potential changes occur in pyruvate entry into the tricarboxylic acid (TCA) cycle during growth. Isolated mitochondria from each muscle were incubated with 13C-labeled metabolites to assess isotopomer enrichment patterns of TCA intermediates. Citrate M + 2 and M + 4 derived from [13C3]-pyruvate increased at 87 d in LAT and MS mitochondria compared to LD mitochondria (p < 0.05). Regardless of the muscle, citrate M+3 increased at 87 d compared to 20, 53, and 120 d, while 180 d showed intermediate values (p < 0.01). These data support the notion that pyruvate metabolism is dynamic during growth. Our findings establish a metabolic fingerprint associated with postnatal muscle hypertrophy. [ABSTRACT FROM AUTHOR]

Published
2024
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6. Cell fusion: Inter-organ tissue communication promotes a union between myoblasts.

Author

Bi, Pengpeng and Geisbrecht, Erika R.

Subjects
*CELL fusion, *MYOBLASTS, *GENE fusion, *GENETIC regulation, *TISSUES, *DROSOPHILA
Abstract

Repeated rounds of fusion between apposing myoblasts allow muscles to become multinucleated. New research finds that myoblasts undergoing fusion in the Drosophila embryo respond to hormone signaling from a nearby tissue, resulting in the activation of a myoblast-specific gene necessary for the fusion process. [ABSTRACT FROM AUTHOR]

Published
2024
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17. Chitin deacetylases are necessary for insect femur muscle attachment and mobility.

Author

Seulgi Mun, Mi Young Noh, Geisbrecht, Erika R., Kramer, Karl J., Muthukrishnan, Subbaratnam, and Yasuyuki Arakane

Subjects
RED flour beetle, CHITIN, DEACETYLASES, ZONA pellucida, FEMUR, LABOR mobility
Abstract

Muscle attachment sites (MASs, apodemes) in insects and other arthropods involve specialized epithelial cells, called tendon cells or tenocytes, that adhere to apical extracellular matrices containing chitin. Here, we have uncovered a function for chitin deacetylases (CDAs) in arthropod locomotion and muscle attachment using a double-stranded RNA-mediated gene-silencing approach targeted toward specific CDA isoforms in the red flour beetle, Tribolium castaneum (Tc). Depletion of TcCDA1 or the alternatively spliced TcCDA2 isoform, TcCDA2a, resulted in internal tendon cuticle breakage at the femur-tibia joint, muscle detachment from both internal and external tendon cells, and defective locomotion. TcCDA deficiency did not affect early muscle development and myofiber growth toward the cuticular MASs but instead resulted in aborted microtubule development, loss of hemiadherens junctions, and abnormal morphology of tendon cells, all features consistent with a loss of tension within and between cells. Moreover, simultaneous depletion of TcCDA1 or TcCDA2a and the zona pellucida domain protein, TcDumpy, prevented the internal tendon cuticle break, further supporting a role for force-dependent interactions between muscle and tendon cells. We propose that in T. castaneum, the absence of N-acetylglucosamine deacetylation within chitin leads to a loss of microtubule organization and reduced membrane contacts at MASs in the femur, which adversely affect musculoskeletal connectivity, force transmission, and physical mobility. [ABSTRACT FROM AUTHOR]

Published
2022
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19. Drosophila ELMO/CED-12 interacts with Myoblast city to direct myoblast fusion and ommatidial organization

Author

Geisbrecht, Erika R., Haralalka, Shruti, Swanson, Selene K., Florens, Laurence, Washburn, Mike P., and Abmayr, Susan M.

Subjects
Drosophila, Biological sciences, Stowers Institute for Medical Research
Abstract

To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.ydbio.2007.11.022 Byline: Erika R. Geisbrecht (a), Shruti Haralalka (a), Selene K. Swanson (b), Laurence Florens (b), Mike P. Washburn (b), Susan M. Abmayr (a) Keywords: Drosophila; ELMO; MBC; Rac; Myoblast fusion; Ommatidial organization Abstract: Members of the CDM (CED-5, Dock180, Myoblast city) superfamily of guanine nucleotide exchange factors function in diverse processes that include cell migration and myoblast fusion. Previous studies have shown that the SH3, DHR1 and DHR2 domains of Myoblast city (MBC) are essential for it to direct myoblast fusion in the Drosophila embryo, while the conserved DCrk-binding proline rich region is expendable. Herein, we describe the isolation of Drosophila ELMO/CED-12, an [approximately equal to]82 kDa protein with a pleckstrin homology (PH) and proline-rich domain, by interaction with the MBC SH3 domain. Mass spectrometry confirms the presence of an MBC/ELMO complex within the embryonic musculature at the time of myoblast fusion and embryos maternally and/or zygotically mutant for elmo exhibit defects in myoblast fusion. Overexpression of MBC and ELMO in the embryonic mesoderm causes defects in myoblast fusion reminiscent of those seen with constitutively-activated Rac1, supporting the previous finding that both the absence of and an excess of Rac activity are deleterious to myoblast fusion. Overexpression of MBC and ELMO/CED-12 in the eye causes perturbations in ommatidial organization that are suppressed by mutations in Rac1 and Rac2, demonstrating genetically that MBC and ELMO/CED-12 cooperate to activate these small GTPases in Drosophila. Author Affiliation: (a) Stowers Institute for Medical Research, 1000 E. 50th St., Kansas City, MO 64110, USA (b) Proteomics Core Facility, Stowers Institute for Medical Research, 1000 E. 50th St, Kansas City, MO 64110, USA Article History: Received 5 October 2007; Revised 7 November 2007; Accepted 17 November 2007

Published
2008

20. Costameric integrin and sarcoglycan protein levels are altered in aDrosophilamodel for Limb-girdle muscular dystrophy type 2H

Author

Bawa, Simranjot, primary, Gameros, Samantha, additional, Baumann, Kenny, additional, Brooks, David S., additional, Kollhoff, Joseph A., additional, Zolkiewski, Michal, additional, Re Cecconi, Andrea David, additional, Panini, Nicolò, additional, Russo, Massimo, additional, Piccirillo, Rosanna, additional, Johnson, David K., additional, Kashipathy, Maithri M., additional, Battaile, Kevin P., additional, Lovell, Scott, additional, Bouyain, Samuel E.A., additional, Kawakami, Jessica, additional, and Geisbrecht, Erika R., additional

Published
2021
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27. Drosophila TRIM32 cooperates with glycolytic enzymes to promote cell growth

Author

Bawa, Simranjot, primary, Brooks, David S, additional, Neville, Kathryn E, additional, Tipping, Marla, additional, Sagar, Md Abdul, additional, Kollhoff, Joseph A, additional, Chawla, Geetanjali, additional, Geisbrecht, Brian V, additional, Tennessen, Jason M, additional, Eliceiri, Kevin W, additional, and Geisbrecht, Erika R, additional

Published
2020
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30. Costameric integrin and sarcoglycan protein levels are altered in a Drosophilamodel for Limb-girdle muscular dystrophy type 2H

Author

Bawa, Simranjot, Gameros, Samantha, Baumann, Kenny, Brooks, David S., Kollhoff, Joseph A., Zolkiewski, Michal, Re Cecconi, Andrea David, Panini, Nicolò, Russo, Massimo, Piccirillo, Rosanna, Johnson, David K., Kashipathy, Maithri M., Battaile, Kevin P., Lovell, Scott, Bouyain, Samuel E.A., Kawakami, Jessica, and Geisbrecht, Erika R.

Abstract

Expression of human disease-causing LGMD2H alleles in Drosophilacauses muscle degeneration and elevated levels of integrin and sarcoglycan costamere proteins, likely exacerbating disease progression.

Published
2021
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32. A role for Drosophila IAP1-mediated caspase inhibition in Rac-dependent cell migration

Author

Geisbrecht, Erika R. and Montell, Denise J.

Subjects
Apoptosis -- Research, Cell migration -- Research, Drosophila -- Genetic aspects, Drosophila -- Research, Genetic research, Biological sciences
Abstract

The migration defect is suppressed due to the overexpression of the Drosophila inhibitor of apoptosis 1 (DIAP1), which is encoded by the thread (th) gene. An apoptosis-independent role for DIAP1-mediated Dronc inhibition in Rac-mediated cell motility is suggested.

Published
2004

38. Genetic Interaction Screens Identify a Role for Hedgehog Signaling in Drosophila Border Cell Migration

Author

Geisbrecht, Erika R., Sawant, Ketki, Su, Ying, Liu, Ze (Cindy), Silver, Debra L., Burtscher, Ashley, Wang, Xuejiao, Zhu, Alan Jian, and McDonald, Jocelyn A.

Subjects
Male, Gene Expression Profiling, Ovary, Gene Expression Regulation, Developmental, Epistasis, Genetic, Article, Animals, Genetically Modified, Drosophila melanogaster, Oogenesis, Cell Movement, Morphogenesis, Animals, Drosophila Proteins, Female, Gene Regulatory Networks, Hedgehog Proteins, Signal Transduction
Abstract

Cell motility is essential for embryonic development and physiological processes such as the immune response, but also contributes to pathological conditions such as tumor progression and inflammation. However, our understanding of the mechanisms underlying migratory processes is incomplete. Drosophila border cells provide a powerful genetic model to identify the roles of genes that contribute to cell migration.Members of the Hedgehog signaling pathway were uncovered in two independent screens for interactions with the small GTPase Rac and the polarity protein Par-1 in border cell migration. Consistent with a role in migration, multiple Hh signaling components were enriched in the migratory border cells. Interference with Hh signaling by several different methods resulted in incomplete cell migration. Moreover, the polarized distribution of E-Cadherin and a marker of tyrosine kinase activity were altered when Hh signaling was disrupted. Conservation of Hh-Rac and Hh-Par-1 signaling was illustrated in the wing, in which Hh-dependent phenotypes were enhanced by loss of Rac or par-1.We identified a pathway by which Hh signaling connects to Rac and Par-1 in cell migration. These results further highlight the importance of modifier screens in the identification of new genes that function in developmental pathways.

Published
2013

39. Identification of CryAB as a target of NUAK kinase activity in Drosophilamuscle tissue

Author

Zhao, Ziwei, Brooks, David, Guo, Yungui, and Geisbrecht, Erika R

Abstract

Phosphorylation reactions performed by protein kinases are one of the most studied post-translational modifications within cells. Much is understood about conserved residues within protein kinase domains that perform catalysis of the phosphotransfer reaction, yet the identity of the target substrates and downstream biological effects vary widely among cells, tissues, and organisms. Here, we characterize key residues essential for NUAK kinase activity in Drosophila melanogastermyogenesis and homeostasis. Creation of a NUAKkinase-dead mutation using Clustered Regularly Interspaced Short Palindromic Repeats (CRISPR)/Cas9 results in lethality at the embryo to larval transition, while loss of NUAK catalytic function later in development produces aggregation of the chaperone protein αB-crystallin/CryAB in muscle tissue. Yeast 2-hybrid assays demonstrate a physical interaction between NUAK and CryAB. We further show that a phospho-mimetic version of NUAK promotes the phosphorylation of CryAB and this post-translational modification occurs at 2 previously unidentified phosphosites that are conserved in the primary sequence of human CryAB. Mutation of these serine residues in D. melanogasterNUAK abolishes CryAB phosphorylation, thus, proving their necessity at the biochemical level. These studies together highlight the importance of kinase activity regulation and provide a platform to further explore muscle tissue proteostasis.

Published
2023
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