@article{ma_shatil-cohen_ben-dor_wigoda_perera_im_diminshtein_yu_boss_moshelion_et al._2014, title={Do phosphoinositides regulate membrane water permeability of tobacco protoplasts by enhancing the aquaporin pathway?}, volume={241}, ISSN={0032-0935 1432-2048}, url={http://dx.doi.org/10.1007/s00425-014-2216-x}, DOI={10.1007/s00425-014-2216-x}, abstractNote={Enhancing the membrane content of PtdInsP 2 , the already-recognized protein-regulating lipid, increased the osmotic water permeability of tobacco protoplasts, apparently by increasing the abundance of active aquaporins in their membranes. While phosphoinositides are implicated in cell volume changes and are known to regulate some ion channels, their modulation of aquaporins activity has not yet been reported for any organism. To examine this, we compared the osmotic water permeability (P f) of protoplasts isolated from tobacco (Nicotiana tabacum) cultured cells (NT1) with different (genetically lowered or elevated relative to controls) levels of inositol trisphosphate (InsP3) and phosphatidyl inositol [4,5] bisphosphate (PtdInsP2). To achieve this, the cells were transformed with, respectively, the human InsP3 5-phosphatase ('Ptase cells') or human phosphatidylinositol (4) phosphate 5-kinase ('PIPK cells'). The mean P f of the PIPK cells was several-fold higher relative to that of controls and Ptase cells. Three results favor aquaporins over the membrane matrix as underlying this excessive P f: (1) transient expression of the maize aquaporin ZmPIP2;4 in the PIPK cells increased P f by 12-30 μm s(-1), while in the controls only by 3-4 μm s(-1). (2) Cytosol acidification-known to inhibit aquaporins-lowered the P f in the PIPK cells down to control levels. (3) The transcript of at least one aquaporin was elevated in the PIPK cells. Together, the three results demonstrate the differences between the PIPK cells and their controls, and suggest a hitherto unobserved regulation of aquaporins by phosphoinositides, which could occur through direct interaction or indirect phosphoinositides-dependent cellular effects.}, number={3}, journal={Planta}, publisher={Springer Science and Business Media LLC}, author={Ma, Xiaohong and Shatil-Cohen, Arava and Ben-Dor, Shifra and Wigoda, Noa and Perera, Imara Y. and Im, Yang Ju and Diminshtein, Sofia and Yu, Ling and Boss, Wendy F. and Moshelion, Menachem and et al.}, year={2014}, month={Dec}, pages={741–755} }
 @article{ischebeck_werner_krishnamoorthy_lerche_meijón_stenzel_löfke_wiessner_im_perera_et al._2013, title={Phosphatidylinositol 4,5-Bisphosphate Influences PIN Polarization by Controlling Clathrin-Mediated Membrane Trafficking in Arabidopsis}, volume={25}, ISSN={1040-4651 1532-298X}, url={http://dx.doi.org/10.1105/tpc.113.116582}, DOI={10.1105/tpc.113.116582}, abstractNote={Abstract}, number={12}, journal={The Plant Cell}, publisher={American Society of Plant Biologists (ASPB)}, author={Ischebeck, Till and Werner, Stephanie and Krishnamoorthy, Praveen and Lerche, Jennifer and Meijón, Mónica and Stenzel, Irene and Löfke, Christian and Wiessner, Theresa and Im, Yang Ju and Perera, Imara Y. and et al.}, year={2013}, month={Dec}, pages={4894–4911} }
 @article{boss_im_2012, title={Phosphoinositide Signaling}, volume={63}, ISSN={["1545-2123"]}, DOI={10.1146/annurev-arplant-042110-103840}, abstractNote={ All things flow and change…even in the stillest matter there is unseen flux and movement. }, journal={ANNUAL REVIEW OF PLANT BIOLOGY, VOL 63}, author={Boss, Wendy F. and Im, Yang Ju}, year={2012}, pages={409–429} }
 @article{boss_sederoff_im_moran_grunden_perera_2010, title={Basal Signaling Regulates Plant Growth and Development}, volume={154}, ISSN={["0032-0889"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-77957739073&partnerID=MN8TOARS}, DOI={10.1104/pp.110.161232}, abstractNote={The term signal transduction refers to the classical paradigm where an external stimulus is sensed and initiates an increase in second messengers. Each second messenger transmits and amplifies the signal by activating a subset of downstream pathways. This complex network of interwoven downstream}, number={2}, journal={PLANT PHYSIOLOGY}, author={Boss, Wendy F. and Sederoff, Heike Winter and Im, Yang Ju and Moran, Nava and Grunden, Amy M. and Perera, Imara Y.}, year={2010}, month={Oct}, pages={439–443} }
 @article{im_ji_lee_killens_grunden_boss_2009, title={Expression of Pyrococcus furiosus Superoxide Reductase in Arabidopsis Enhances Heat Tolerance}, volume={151}, ISSN={["1532-2548"]}, DOI={10.1104/pp.109.145409}, abstractNote={Abstract}, number={2}, journal={PLANT PHYSIOLOGY}, author={Im, Yang Ju and Ji, Mikyoung and Lee, Alice and Killens, Rushyannah and Grunden, Amy M. and Boss, Wendy F.}, year={2009}, month={Oct}, pages={893–904} }
 @article{ma_shor_diminshtein_yu_im_perera_lomax_boss_moran_2009, title={Phosphatidylinositol (4,5)Bisphosphate Inhibits K+-Efflux Channel Activity in NT1 Tobacco Cultured Cells}, volume={149}, ISSN={["1532-2548"]}, DOI={10.1104/pp.108.129007}, abstractNote={Abstract}, number={2}, journal={PLANT PHYSIOLOGY}, author={Ma, Xiaohong and Shor, Oded and Diminshtein, Sofia and Yu, Ling and Im, Yang Ju and Perera, Imara and Lomax, Aaron and Boss, Wendy F. and Moran, Nava}, year={2009}, month={Feb}, pages={1127–1140} }
 @article{davis_im_dubin_tomer_boss_2007, title={Arabidopsis phosphatidylinositol phosphate kinase 1 binds F-actin and recruits phosphatidylinositol 4-kinase beta 1 to the actin cytoskeleton (Retracted article. See vol. 284, pg. 16060, 2009)}, volume={282}, ISSN={["1083-351X"]}, DOI={10.1074/jbc.M611728200}, abstractNote={The actin cytoskeleton can be influenced by phospholipids and lipid-modifying enzymes. In animals the phosphatidylinositol phosphate kinases (PIPKs) are associated with the cytoskeleton through a scaffold of proteins; however, in plants such an interaction was not clear. Our approach was to determine which of the plant PIPKs interact with actin and determine whether the PIPK-actin interaction is direct. Our results indicate that <i>At</i>PIPK1 interacts directly with actin and that the binding is mediated through a predicted linker region in the lipid kinase. <i>At</i>PIPK1 also recruits <i>At</i>PI4Kβ1 to the cytoskeleton. Recruitment of <i>At</i>PI4Kβ1 to F-actin was dependent on the C-terminal catalytic domain of phosphatidylinositol-4-phosphate 5-kinase but did not require the presence of the N-terminal 251 amino acids, which includes 7 putative membrane occupation and recognition nexus motifs. <i>In vivo</i> studies confirm the interaction of plant lipid kinases with the cytoskeleton and suggest a role for actin in targeting PIPKs to the membrane.}, number={19}, journal={JOURNAL OF BIOLOGICAL CHEMISTRY}, author={Davis, Amanda J. and Im, Yang Ju and Dubin, Joshua S. and Tomer, Kenneth B. and Boss, Wendy F.}, year={2007}, month={May}, pages={14121–14131} }
 @article{im_perera_brglez_davis_stevenson-paulik_phillippy_johannes_allen_boss_2007, title={Increasing plasma membrane phosphatidylinositol(4,5)bisphosphate biosynthesis increases phosphoinositide metabolism in Nicotiana tabacum}, volume={19}, ISSN={["1532-298X"]}, DOI={10.1105/tpc.107.051367}, abstractNote={Abstract}, number={5}, journal={PLANT CELL}, author={Im, Yang Ju and Perera, Imara Y. and Brglez, Irena and Davis, Amanda J. and Stevenson-Paulik, Jill and Phillippy, Brian Q. and Johannes, Eva and Allen, Nina S. and Boss, Wendy F.}, year={2007}, month={May}, pages={1603–1616} }
 @article{im_davis_perera_johannes_allen_boss_2007, title={The N-terminal membrane occupation and recognition nexus domain of Arabidopsis phosphatidylinositol phosphate kinase 1 regulates enzyme activity}, volume={282}, ISSN={["1083-351X"]}, DOI={10.1074/jbc.M611342200}, abstractNote={The type I B family of phosphatidylinositol phosphate kinases (PIPKs) contain a characteristic region of Membrane Occupation and Recognition Nexus (MORN) motifs at the N terminus. These MORN motifs are not found in PIPKs from other eukaryotes. To understand the impact of the additional N-terminal domain on protein function and subcellular distribution, we expressed truncated and full-length versions of AtPIPK1, one member of this family of PIPKs, in Escherichia coli and in tobacco cells grown in suspension culture. Deletion of the N-terminal MORN domain (amino acids 1–251) of AtPIPK1 increased the specific activity of the remaining C-terminal peptide (ΔMORN) >4-fold and eliminated activation by phosphatidic acid (PtdOH). PtdOH activation could also be eliminated by mutating Pro396 to Ala (P396A) in the predicted linker region between the MORN and the kinase homology domains. AtPIPK1 is product-activated and the MORN domain binds PtdIns(4,5)P2. Adding back the MORN peptide to ΔMORN or to the PtdOH-activated full-length protein increased activity ∼2-fold. Furthermore, expressing the MORN domain in vivo increased the plasma membrane PtdInsP kinase activity. When cells were exposed to hyperosmotic stress, the MORN peptide redistributed from the plasma membrane to a lower phase or endomembrane fraction. In addition, endogenous PtdInsP kinase activity increased in the endomembrane fraction of hyperosmotically stressed cells. We conclude that the MORN peptide can regulate both the function and distribution of the enzyme in a manner that is sensitive to the lipid environment.}, number={8}, journal={JOURNAL OF BIOLOGICAL CHEMISTRY}, author={Im, Yang Ju and Davis, Amanda J. and Perera, Imara Y. and Johannes, Eva and Allen, Nina S. and Boss, Wendy F.}, year={2007}, month={Feb}, pages={5443–5452} }
 @article{perera_davis_galanopilou_im_boss_2005, title={Characterization and comparative analysis of Arabidopsis phosphatidylinositol phosphate 5-kinase 10 reveals differences in Arabidopsis and human phosphatidylinositol phosphate kinases}, volume={579}, ISSN={["1873-3468"]}, DOI={10.1016/j.febslet.2005.05.018}, abstractNote={
Arabidopsis phosphatidylinositol phosphate (PtdInsP) kinase 10 (AtPIPK10; At4g01190) is shown to be a functional enzyme of the subfamily A, type I AtPtdInsP kinases. It is biochemically distinct from AtPIPK1 (At1g21980), the only other previously characterized AtPtdInsP kinase which is of the B subfamily. AtPIPK10 has the same K
m, but a 10‐fold lower V
max than AtPIPK1 and it is insensitive to phosphatidic acid. AtPIPK10 transcript is most abundant in inflorescence stalks and flowers, whereas AtPIPK1 transcript is present in all tissues. Comparative analysis of recombinant AtPIPK10 and AtPIPK1 with recombinant HsPIPKIα reveals that the Arabidopsis enzymes have roughly 200‐ and 20‐fold lower V
max/K
m, respectively. These data reveal one explanation for the longstanding mystery of the relatively low phosphatidylinositol‐(4,5)‐bisphosphate:phosphatidylinositol‐4‐phosphate ratio in terrestrial plants.}, number={16}, journal={FEBS LETTERS}, author={Perera, IY and Davis, AJ and Galanopilou, D and Im, YJ and Boss, WF}, year={2005}, month={Jun}, pages={3427–3432} }
 @article{im_ji_lee_boss_grunden_2005, title={Production of a thermostable archaeal superoxide reductase in plant cells}, volume={579}, ISSN={["1873-3468"]}, DOI={10.1016/j.febslet.2005.09.015}, abstractNote={
Pyrococcus furiosus superoxide reductase (SOR) is a thermostable archaeal enzyme that reduces superoxide without producing oxygen. When produced as a fusion protein with the green fluorescent protein in plant cells, P. furiosus SOR is located in the cytosol and nucleus. The recombinant SOR enzyme retains its function and heat stability when assayed in vitro. Importantly, expressing SOR in plant cells enhances their survival at high temperature indicating that it functions in vivo. The archaeal SOR provides a novel mechanism to reduce superoxide and demonstrates the potential for using archaeal genes to alter eukaryotic metabolism.}, number={25}, journal={FEBS LETTERS}, author={Im, YJ and Ji, MK and Lee, AM and Boss, WF and Grunden, AM}, year={2005}, month={Oct}, pages={5521–5526} }