Objects as culture-specific referents of color terms in Russian

The present study is an extension of our analysis of Russian basic color terms (BCTs) elicited in a web-based psycholinguistic experiment. Color samples (N = 600) were approximately uniformly distributed in the Munsell color solid. An unconstrained color-naming method was employed. Native Russian speakers (N = 713; 333 males) participated in the study. Among 1422 elicited unique color words, 698 terms (49%) were derived from object names. Here we explore object-derived non-BCTs, focusing on broad classes of names referred to objects, categories within these, and the inventory of color terms, as well as their frequency, patterns of derivation, and derivational productivity. Six classes of object referents were identified: flora, fauna, inanimate nature, food and beverages, man-made objects, body and bodily products. In detail, 20 most frequent object-derived terms are reported. These are accompanied by analysis of gender differences and representation of the terms' denotata on the Munsell Mercator projection. In addition, Russian object-derived color terms are related to those in English; discussed are differences between the 2 languages in the color term classes, inventories and incidences. We conclude that Russian object-derived color terms follow the generic metonymy pattern, that is, signifying color of objects in the speakers' natural environment. The inventory is also language-specific, reflecting social practices, preferences and views entrenched in the traditional Russian culture. Furthermore, recent extensive development of the inventory signals 2 novel phenomena: marked globalization influence, surfacing as abundant transliteration of English referent loanwords, and noticeable sociolectal diversification that manifests itself by novel evocative color terms, particularly in marketing and advertisement

Guard cell anion channel SLAC1 is regulated by CDPK protein kinases with distinct Ca2+ affinities

In response to drought stress, the phytohormone abscisic acid (ABA) induces stomatal closure. Thereby the stress hormone activates guard cell anion channels in a calcium-dependent, as well as –independent, manner. Open stomata 1 protein kinase (OST1) and ABI1 protein phosphatase (ABA insensitive 1) represent key components of calcium-independent ABA signaling. Recently, the guard cell anion channel SLAC1 was identified. When expressed heterologously SLAC1 remained electrically silent. Upon coexpression with Ca2+-independent OST1, however, SLAC1 anion channels appear activated in an ABI1-dependent manner. Mutants lacking distinct calcium-dependent protein kinases (CPKs) appeared impaired in ABA stimulation of guard cell ion channels, too. To study SLAC1 activation via the calcium-dependent ABA pathway, we studied the SLAC1 response to CPKs in the Xenopus laevis oocyte system. Split YFP-based protein–protein interaction assays, using SLAC1 as the bait, identified guard cell expressed CPK21 and 23 as major interacting partners. Upon coexpression of SLAC1 with CPK21 and 23, anion currents document SLAC1 stimulation by these guard cell protein kinases. Ca2+-sensitive activation of SLAC1, however, could be assigned to the CPK21 pathway only because CPK23 turned out to be rather Ca2+-insensitive. In line with activation by OST1, CPK activation of the guard cell anion channel was suppressed by ABI1. Thus the CPK and OST1 branch of ABA signal transduction in guard cells seem to converge on the level of SLAC1 under the control of the ABI1/ABA-receptor complex

Activity of guard cell anion channel SLAC1 is controlled by drought-stress signaling kinase-phosphatase pair

In response to drought stress the phytohormone ABA (abscisic acid) induces stomatal closure and, therein, activates guard cell anion channels in a calcium-dependent as well as-independent manner. Two key components of the ABA signaling pathway are the protein kinase OST1 (open stomata 1) and the protein phosphatase ABI1 (ABA insensitive 1). The recently identified guard cell anion channel SLAC1 appeared to be the key ion channel in this signaling pathway but remained electrically silent when expressed heterologously. Using split YFP assays, we identified OST1 as an interaction partner of SLAC1 and ABI1. Upon coexpression of SLAC1 with OST1 in Xenopus oocytes, SLAC1-related anion currents appeared similar to those observed in guard cells. Integration of ABI1 into the SLAC1/OST1 complex, however, prevented SLAC1 activation. Our studies demonstrate that SLAC1 represents the slow, deactivating, weak voltage-dependent anion channel of guard cells controlled by phosphorylation/dephosphorylation