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Takeshi Sasaki,Shota Jikumaru,Wakana Azuma,Keiko Kuroda,Hiroaki Ishii 한국산림과학회 2016 Forest Science And Technology Vol.12 No.3
The larvae of Japanese gypsy moth (JGM, Lymantria dispar japonica) are highly polyphagous and considered a serious pest that cause significant ecological and economic losses in forests. Monitoring of egg masses is important to prevent large outbreaks of JGM from occurring in their native range. To investigate oviposition site selection by JGM, we analyzed the occurrence and spatial distribution of egg masses across various evergreen tree species within a secondary forest dominated by evergreen broad-leaved trees in western Japan, following a large outbreak. Egg masses were concentrated on the abaxial surfaces of the leaves of a few evergreen tree species. There was a strong preference for Camellia japonica L., on which more than 75% of the egg masses were found. Egg masses were only found on evergreen tree species with large leaves (leaf area >10 cm2 and leaf dry mass >0.1 g). The spatial distribution of egg masses were clustered at scales around 1‒2 m. For effective monitoring of JGM egg masses in warm-temperate evergreen broad-leaved forests of Japan, the abaxial surfaces of the most abundant evergreen broadleaved trees with large leaves should be checked. If egg masses are found, it is likely that nearby trees of the same species
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Yamamoto, Yukio,Lee, Dongwon,Kim, Yoonhee,Lee, Bokyoung,Seo, Changwoo,Kawasaki, Hiroshi,Kuroda, Shinya,Tanaka-Yamamoto, Keiko The Society 2012 The Journal of neuroscience Vol.32 No.41
<P>It was demonstrated previously that a positive feedback loop, including protein kinase C (PKC) and mitogen-activated protein kinase (MAPK), is required for the gradual expression of cerebellar long-term depression (LTD). PKC and MAPK are mutually activated in this loop. MAPK-dependent PKC activation is likely to be mediated by phospholipase A2. On the other hand, it is not clear how PKC activates MAPK. Therefore, the entire picture of this loop was not fully understood. We here test the hypothesis that this loop is completed by the PKC substrate, Raf kinase inhibitory protein (RKIP). To test this hypothesis, we used a mutant form of RKIP that is not phosphorylated by PKC and thus constitutively inhibits Raf-1 and MEK, upstream kinases of MAPK. When this RKIP mutant was introduced into Purkinje cells of mouse cerebellar slices through patch-clamp electrodes, LTD was blocked, while wild-type (WT) RKIP had no effect on LTD. Physiological epistasis experiments demonstrated that RKIP works downstream of PKC and upstream of MAPK during LTD induction. Furthermore, biochemical analyses demonstrated that endogenous RKIP dissociates from Raf-1 and MEK during LTD induction in a PKC-dependent manner, suggesting that RKIP binding-dependent inhibition of Raf-1 and MEK is removed upon LTD induction. We therefore conclude that PKC-dependent regulation of RKIP leads to MAPK activation, with RKIP completing the positive feedback loop that is required for LTD.</P>
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