70 research outputs found
The overwintering of Antarctic krill, Euphausia superba, from an ecophysiological perspective
A major aim of this review is to determine
which physiological functions are adopted by adults and
larvae to survive the winter season with low food supply
and their relative importance. A second aim is to clarify the
extent to which seasonal variation in larval and adult krill
physiology is mediated by environmental factors with a
strong seasonality, such as food supply or day light. Experimental
studies on adult krill have demonstrated that speciWc
physiological adaptations during autumn and winter,
such as reduced metabolic rates and feeding activity, are
not caused simply by the scarcity of food, as was previously
assumed. These adaptations appear to be inXuenced
by the local light regime. The physiological functions that
larval krill adopt during winter (reduced metabolism,
delayed development, lipid utilisation, and variable growth
rates) are, in contrast to the adults, under direct control by
the available food supply. During winter, the adults often
seem to have little association with sea ice (at least until
early spring). The larvae, however, feed within sea ice but
mainly on the grazers of the ice algal community rather
than on the algae themselves. In this respect, a miss-match
in timing of the occurrence of the last phytoplankton
blooms in autumn and the start of the sea ice formation, as
has been increasingly observed in the west Antarctic Peninsula
(WAP) region, will impact larval krill development
during winter in terms of food supply and consequently the
krill stock in this region
RhoE function is regulated by ROCK I-mediated phosphorylation
The Rho GTPase family member RhoE regulates actin filaments partly by binding to and inhibiting ROCK I, a serine/threonine kinase that induces actomyosin contractility. Here, we show that ROCK I can phosphorylate multiple residues on RhoE in vitro. In cells, ROCK I-phosphorylated RhoE localizes in the cytosol, whereas unphosphorylated RhoE is primarily associated with membranes. Phosphorylation has no effect on RhoE binding to ROCK I, but instead increases RhoE protein stability. Using phospho-specific antibodies, we show that ROCK phosphorylates endogenous RhoE at serine 11 upon cell stimulation with platelet-derived growth factor, and that this phosphorylation requires an active protein kinase C signalling pathway. In addition, we demonstrate that phosphorylation of RhoE correlates with its activity in inducing stress fibre disruption and inhibiting Ras-induced transformation. This is the first demonstration of an endogenous Rho family member being phosphorylated in vivo and indicates that phosphorylation is an important mechanism to control the stability and function of this GTPase-deficient Rho protein
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