@article{lin_fang_park_crews_adler_2010, title={MARCKS and Related Chaperones Bind to Unconventional Myosin V Isoforms in Airway Epithelial Cells}, volume={43}, ISSN={["1535-4989"]}, DOI={10.1165/rcmb.2010-0016rc}, abstractNote={We have shown previously that myristoylated alanine-rich C kinase substrate (MARCKS) is a key regulatory molecule in the process of mucin secretion by airway epithelial cells, and that part of the secretory mechanism involves intracellular associations of MARCKS with specific chaperones: heat shock protein 70 (Hsp70) and cysteine string protein (CSP). Here, we report that MARCKS also interacts with unconventional myosin isoforms within these cells, and further molecular interactions between MARCKS and these chaperones/cytoskeletal proteins are elucidated. Primary human bronchial epithelial cells and the HBE1 cell line both expressed myosin V and VI proteins, and both MARCKS and CSP were shown to bind to myosin V, specifically Va and Vc. This binding was enhanced by exposing the cells to phorbol-12-myristate-13-acetate, an activator of protein kinase C and stimulator of mucin secretion. Binding of MARCKS, Hsp70, and CSP was further investigated by His-tagged pull down assays of purified recombinant proteins and multiple transfections of HBE1 cells with fusion proteins (MARCKS-HA; Flag-Hsp70; c-Myc-CSP) and immunoprecipitation. The results showed that MARCKS binds directly to Hsp70, and that Hsp70 binds directly to CSP, but that MARCKS binding to CSP appears to require the presence of Hsp70. Interrelated binding(s) of MARCKS, chaperones, and unconventional myosin isoforms may be integral to the mucin secretion process.}, number={2}, journal={AMERICAN JOURNAL OF RESPIRATORY CELL AND MOLECULAR BIOLOGY}, author={Lin, Ko-Wei and Fang, Shijing and Park, Joungjoa and Crews, Anne L. and Adler, Kenneth B.}, year={2010}, month={Aug}, pages={131–136} }
 @article{lin_j. j._s._adler_2008, title={MARCKS protein regulation of mucin secretion in airway epithelial cells: binding of MARCKS to chaperones and to MyosinV.}, volume={177}, journal={American Journal of Respiratory and Critical Care Medicine}, author={Lin, K. Park and J. J., Fang and S. and Adler, K. B.}, year={2008}, pages={A993} }
 @article{park_fang_crews_lin_adler_2008, title={MARCKS regulation of mucin secretion by airway epithelial cells in vitro: interactions with chaperone proteins.}, volume={102}, journal={American Journal of Respiratory Cell and Molecular Biology}, author={Park, J. J. and Fang, S. and Crews, A. L. and Lin, K.-W. and Adler, K. B.}, year={2008}, pages={949–955} }
 @article{park_fang_crews_lin_adler_2008, title={MARCKS regulation of mucin secretion by airway epithelium in vitro - Interaction with chaperones}, volume={39}, DOI={10.1165/rcm6.2007-0139OC}, number={1}, journal={American Journal of Respiratory Cell and Molecular Biology}, author={Park, J. and Fang, S. J. and Crews, A. L. and Lin, K. W. and Adler, K. B.}, year={2008}, pages={68–76} }
 @misc{lin_park_crews_li_adler_2008, title={Protease-activated receptor-2 (PAR-2) is a weak enhancer of mucin secretion by human bronchial epithelial cells in vitro}, volume={40}, ISSN={["1878-5875"]}, DOI={10.1016/j.biocel.2007.10.031}, abstractNote={PAR-2, a member of a family of G-protein-coupled receptors, can be activated by serine proteases via proteolytic cleavage. PAR-2 expression is known to be upregulated in respiratory epithelium subsequent to inflammation in asthma and chronic obstructive pulmonary disease (COPD). Since these diseases also are characterized by excessive mucus production and secretion, we investigated whether PAR-2 could be linked to mucin hypersecretion by airway epithelium. Normal human bronchial epithelial (NHBE) cells in primary culture or the human bronchial epithelial cell lines, NCI-H292 and HBE-1, were used. NHBE, NCI-H292, and HBE-1 cells expressed prominent levels of PAR-2 protein. Short-term (30min) exposure of cells to the synthetic PAR-2 agonist peptide (SLIGKV-NH2) elicited a small but statistically significant increase in mucin secretion at high concentrations (100microM and 1000microM), compared to a control peptide with reversed amino acid sequence (VKGILS-NH2). Neither human lung tryptase nor bovine pancreatic trypsin, both PAR-2 agonists, affected NHBE cell mucin secretion when added over a range of concentrations. Knockdown of PAR-2 expression by siRNA blocked the stimulatory effect of the AP. The results suggest that, since PAR-2 activation only weakly increases mucin secretion by human airway epithelial cells in vitro, PAR-2 probably is not a significant contributor to mucin hypersecretion in inflamed airways.}, number={6-7}, journal={INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY}, author={Lin, Ko-Wei and Park, Joungjoa and Crews, Anne L. and Li, Yuehua and Adler, Kenneth B.}, year={2008}, pages={1379–1388} }
 @article{raiford_lin_park_fang_crews_adler_2007, title={Proteomic analysis of mucin granule membrane-associated proteins in human airway epithelial cells: a mechanistic link between MARCKS and hClCA1?}, volume={175}, journal={404nOtfound}, author={Raiford, K. L. and Lin, K. W. and Park, J. and Fang, S. and Crews, A. L. and Adler, K. B.}, year={2007}, pages={A511} }
 @article{adler_fang_lin_park_2006, title={Mechanisms of mucus secretion in the airways.}, volume={2}, DOI={10.1080/17471060500462450}, journal={404nOtfound}, author={Adler, K. B. and Fang, S. and Lin, K-W. and Park, J.}, year={2006}, pages={24–29} }
 @article{lin_park_li_adler_2003, title={Activation of protease-activated receptors?2 (PAR-2) is not associated with enhanced mucin secretion by well-differentiated normal human bronchial epithelial cells in vitro.}, volume={167}, journal={American Journal of Respiratory and Critical Care Medicine}, author={Lin, K. W. and Park, J. J. and Li, Y. and Adler, K. B.}, year={2003}, pages={A204} }