ArticleAmerican journal of respiratory cell and molecular biology2010
MARCKS and related chaperones bind to unconventional myosin V isoforms in airway epithelial cells.
Article in American journal of respiratory cell and molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Neutrophil elastase promotes mucin secretion in airway epithelial cells through the MARCKS/ACK1/cortactin pathway.Central-European journal of immunology · 2025Article
- MARCKS and Lung Disease.American journal of respiratory cell and molecular biology · 2019Review
- Regulated mucin secretion from airway epithelial cells.Frontiers in endocrinology · 2013Review
- Multiple roles for the actin cytoskeleton during regulated exocytosis.Cellular and molecular life sciences : CMLS · 2013Review
- Neutrophil elastase induces MUC5AC secretion via protease-activated receptor 2.Molecular and cellular biochemistry · 2013Article
- MARCKS and HSP70 interactions regulate mucin secretion by human airway epithelial cells in vitro.American journal of physiology. Lung cellular and molecular physiology · 2013Article
- Calpain and MARCKS protein regulation of airway mucin secretion.Pulmonary pharmacology & therapeutics · 2012Article
- Regulation of mucin secretion and inflammation in asthma: a role for MARCKS protein?Biochimica et biophysica acta · 2011Review
- Mucin granule-associated proteins in human bronchial epithelial cells: the airway goblet cell "granulome".Respiratory research · 2011Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
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.
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