Tissue specific expression of Myosin IC Isoforms

Abstract

BackgroundMyosin IC is a single headed member of the myosin superfamily that localizes to the cytoplasm and the nucleus and is implicated in a variety of processes in both compartments. We recently identified a novel isoform of myosin IC and showed that the MYOIC gene in mammalian cells encodes three isoforms (isoforms A, B, and C) that differ only in the addition of short isoform-specific N-terminal peptides. The expression pattern of the isoforms and the mechanisms of expression regulation remain unknown.ResultsTo determine the expression patterns of myosin IC isoforms, we performed a comprehensive expression analysis of the two myosin IC isoforms (isoform A and B) that contain isoform-specific sequences. By immunoblotting with isoform-specific antibodies and by qRT-PCR with isoform-specific primer we demonstrate that myosin IC isoforms A and B have distinct expression patterns in mouse tissues. Specifically, we show that myosin IC isoform A is expressed in a tissue specific pattern, while myosin IC isoform B is ubiquitously expressed at comparable levels in mouse tissues.ConclusionsThe differences in the expression profile of the myosin IC isoforms indicate a tissue-specific MYOIC gene regulation and further suggest that the myosin IC isoforms, despite their high sequence homology, might have tissue-specific and isoform-specific functions.

Selective Expression of Myosin IC Isoform A in Mouse and Human Cell Lines and Mouse Prostate Cancer Tissues

“…This is particularly interesting because our previous analysis of mouse tissue and organs showed a very low expression of myosin IC isoform A in normal mouse prostate [18]. In combination with the the low expression levels of isoform A in the human normal prostate cell line RWPE-1, these data suggest that changes in myosin IC isoform A expression could be associated with the development of prostate cancer.…”

An improved method for RNA extraction from common bean seeds and validation of reference genes for qPCR

“…In a previous study, two β-tubulin genes (Tub8 and Tub9) were not selected as reference genes (Borges et al 2012), suggesting that the β-tubulin isoforms may have different expression patterns, as seen for other enzymes (Sielski et al 2014). In addition, the genes PvAct and Pv18S were the least stable, in accordance with previous studies (Fernandez et al 2011).…”

Myosin-I molecular motors at a glance

“…For instance, the individual overexpression of Myo1a, Myo1b, Myo1c, Myo1d, or Myo1e causes an increase in the force required to pull a tether from (see supplemental table). Myo1b, Myo1c, and Myo1e are widely expressed and found in most cell types (Krendel et al, 2009;Ruppert et al, 1993;Sherr et al, 1993;Sielski et al, 2014;Skowron et al, 1998;Tyska et al, 2005). Loss of Myo1c or Myo1e is associated with kidney disease (Arif et al, 2011;Bi et al, 2013;Krendel et al, 2009;Mele et al, 2011;Wagner et al, 2005), in addition to deafness associated with Myo1c loss (Batters et al, 2004;Holt et al, 2002) and arteriosclerosis upon loss of Myo1e (Inouye et al, 2012).…”

“…Higher vertebrates express eight different myosin-I genes Myo1a-Myo1h, with the corresponding proteins named Myo1a-Myo1h (for a discussion of myosin-I gene and protein nomenclature, see Gillespie et al, 2001) (see poster and Box 1 for more information about phylogenetic sorting). Myosin-I molecular motors are comprised of a motor domain that binds to and interacts with actin in response to ATPase cycling, a light-chain-binding domain (LCBD) that binds one to six Ca 2+ -sensitive calmodulin or calmodulin-like light chains and functions as a lever arm (Bähler et al, 1994;Köhler et al, 2005;Lin et al, 2005;Manceva et al, 2007;McConnell and Tyska, 2010;Ruppert et al, 1993;Sherr et al, 1993;Sielski et al, 2014;Stöffler and Bähler, 1998;Swanljung-Collins and Collins, 1991), and a tail domain (see Structural and kinetic features panel on poster). The tail domain is composed of a myosin-I family tail homology 1 (TH1) domain, which includes a pleckstrin homology (PH) domain known to bind a variety of anionic phospholipids (Adams and Pollard, 1989;Doberstein and Pollard, 1992;Feeser et al, 2010;Hayden et al, 1990;Miyata et al, 1989).…”