@article{nixon_mansouri_singh_du_davis_lee_slabaugh_vandavasi_o’neill_roberts_et al._2016, title={Comparative Structural and Computational Analysis Supports Eighteen Cellulose Synthases in the Plant Cellulose Synthesis Complex}, volume={6}, ISSN={2045-2322}, url={http://dx.doi.org/10.1038/srep28696}, DOI={10.1038/srep28696}, abstractNote={Abstract}, number={1}, journal={Scientific Reports}, publisher={Springer Science and Business Media LLC}, author={Nixon, B. Tracy and Mansouri, Katayoun and Singh, Abhishek and Du, Juan and Davis, Jonathan K. and Lee, Jung-Goo and Slabaugh, Erin and Vandavasi, Venu Gopal and O’Neill, Hugh and Roberts, Eric M. and et al.}, year={2016}, month={Jun} }
 @article{sethaphong_davis_slabaugh_singh_haigler_yingling_2016, title={Prediction of the structures of the plant-specific regions of vascular plant cellulose synthases and correlated functional analysis}, volume={23}, ISSN={0969-0239 1572-882X}, url={http://dx.doi.org/10.1007/s10570-015-0789-6}, DOI={10.1007/s10570-015-0789-6}, number={1}, journal={Cellulose}, publisher={Springer Science and Business Media LLC}, author={Sethaphong, Latsavongsakda and Davis, Jonathan K. and Slabaugh, Erin and Singh, Abhishek and Haigler, Candace H. and Yingling, Yaroslava G.}, year={2016}, month={Feb}, pages={145–161} }
 @article{slabaugh_scavuzzo-duggan_chaves_wilson_wilson_davis_cosgrove_anderson_roberts_haigler_2015, title={The valine and lysine residues in the conserved FxVTxK motif are important for the function of phylogenetically distant plant cellulose synthases}, volume={26}, ISSN={0959-6658 1460-2423}, url={http://dx.doi.org/10.1093/glycob/cwv118}, DOI={10.1093/glycob/cwv118}, abstractNote={Cellulose synthases (CESAs) synthesize the β-1,4-glucan chains that coalesce to form cellulose microfibrils in plant cell walls. In addition to a large cytosolic (catalytic) domain, CESAs have eight predicted transmembrane helices (TMHs). However, analogous to the structure of BcsA, a bacterial CESA, predicted TMH5 in CESA may instead be an interfacial helix. This would place the conserved FxVTxK motif in the plant cell cytosol where it could function as a substrate-gating loop as occurs in BcsA. To define the functional importance of the CESA region containing FxVTxK, we tested five parallel mutations in Arabidopsis thaliana CESA1 and Physcomitrella patens CESA5 in complementation assays of the relevant cesa mutants. In both organisms, the substitution of the valine or lysine residues in FxVTxK severely affected CESA function. In Arabidopsis roots, both changes were correlated with lower cellulose anisotropy, as revealed by Pontamine Fast Scarlet. Analysis of hypocotyl inner cell wall layers by atomic force microscopy showed that two altered versions of Atcesa1 could rescue cell wall phenotypes observed in the mutant background line. Overall, the data show that the FxVTxK motif is functionally important in two phylogenetically distant plant CESAs. The results show that Physcomitrella provides an efficient model for assessing the effects of engineered CESA mutations affecting primary cell wall synthesis and that diverse testing systems can lead to nuanced insights into CESA structure-function relationships. Although CESA membrane topology needs to be experimentally determined, the results support the possibility that the FxVTxK region functions similarly in CESA and BcsA.}, number={5}, journal={Glycobiology}, publisher={Oxford University Press (OUP)}, author={Slabaugh, Erin and Scavuzzo-Duggan, Tess and Chaves, Arielle and Wilson, Liza and Wilson, Carmen and Davis, Jonathan K and Cosgrove, Daniel J and Anderson, Charles T and Roberts, Alison W and Haigler, Candace H}, year={2015}, month={Dec}, pages={509–519} }
 @article{slabaugh_davis_haigler_yingling_zimmer_2014, title={Cellulose synthases: new insights from crystallography and modeling}, volume={19}, ISSN={1360-1385}, url={http://dx.doi.org/10.1016/j.tplants.2013.09.009}, DOI={10.1016/j.tplants.2013.09.009}, abstractNote={•A crystal structure and a modeled structure of cellulose synthases are examined. •We explore similarities/differences between bacterial and plant cellulose synthase. •Molecular mechanisms for known cellulose synthase missense mutations are proposed. •We predict specific residues putatively involved in glucan translocation in plants. Detailed information about the structure and biochemical mechanisms of cellulose synthase (CelS) proteins remained elusive until a complex containing the catalytic subunit (BcsA) of CelS from Rhodobacter sphaeroides was crystalized. Additionally, a 3D structure of most of the cytosolic domain of a plant CelS (GhCESA1 from cotton, Gossypium hirsutum) was produced by computational modeling. This predicted structure contributes to our understanding of how plant CelS proteins may be similar and different as compared with BcsA. In this review, we highlight how these structures impact our understanding of the synthesis of cellulose and other extracellular polysaccharides. We show how the structures can be used to generate hypotheses for experiments testing mechanisms of glucan synthesis and translocation in plant CelS. Detailed information about the structure and biochemical mechanisms of cellulose synthase (CelS) proteins remained elusive until a complex containing the catalytic subunit (BcsA) of CelS from Rhodobacter sphaeroides was crystalized. Additionally, a 3D structure of most of the cytosolic domain of a plant CelS (GhCESA1 from cotton, Gossypium hirsutum) was produced by computational modeling. This predicted structure contributes to our understanding of how plant CelS proteins may be similar and different as compared with BcsA. In this review, we highlight how these structures impact our understanding of the synthesis of cellulose and other extracellular polysaccharides. We show how the structures can be used to generate hypotheses for experiments testing mechanisms of glucan synthesis and translocation in plant CelS.}, number={2}, journal={Trends in Plant Science}, publisher={Elsevier BV}, author={Slabaugh, Erin and Davis, Jonathan K. and Haigler, Candace H. and Yingling, Yaroslava G. and Zimmer, Jochen}, year={2014}, month={Feb}, pages={99–106} }