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A more recent version of this article appeared on February 1, 2004
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Submitted on July 17, 2003
Revised on October 8, 2003
Accepted on November 7, 2003
1 Albany Medical Center; Center for Cardiovascular Sciences, ME 418; 47 New Scotland Av.; Albany, NY 12208
* Corresponding author. E-mail address: barrosm{at}mail.amc.edu.
We have reported that p22, an N-myristoylated EF-hand Ca2+-binding protein, associates with microtubules and plays a role in membrane trafficking. Here, we show that p22 also associates with membranes of the early secretory pathway membranes, in particular ER. On binding of Ca2+, p22’s ability to associate with membranes increases in an N-myristoylation dependent-manner, which is suggestive of a nonclassical Ca2+-myristoyl switch mechanism. To address the intracellular functions of p22, a digitonin-based ‘bulk microinjection’ assay was developed to load cells with anti-p22, wild-type or mutant p22 proteins. Antibodies against a p22 peptide induce microtubule depolymerization and ER fragmentation; this antibody-mediated effect is overcome by preincubation with the respective p22 peptide. In contrast, N-myristoylated p22 induces the formation of microtubule bundles, the accumulation of ER structures along the bundles as well as an increase in ER network formation. An N-myristoylated Ca2+-binding p22 mutant, which is unable to undergo Ca2+-mediated conformational changes, induces microtubule bundling and accumulation of ER structures along the bundles but does not increase ER network formation. Together, these data strongly suggest that p22 modulates the organization and dynamics of microtubule cytoskeleton in a Ca2+-independent manner and affects ER network assembly in a Ca2+-dependent manner.
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