Lateralized gustatory behavior of C. elegans is controlled by specific receptor-type guanylyl cyclases.
Lateralized gustatory behavior of C. elegans is controlled by specific receptor-type guanylyl cyclases.
复制标题
DOI:
10.1016/j.cub.2009.05.043
复制
发表时间:
2009-06-23
期刊:
影响因子:
--
通讯作者:
Hobert O
中科院分区:
文献类型:
--
作者:
Ortiz CO;Faumont S;Takayama J;Ahmed HK;Goldsmith AD;Pocock R;McCormick KE;Kunimoto H;Iino Y;Lockery S;Hobert O
Even though functional lateralization is a predominant feature of many nervous systems, it is poorly understood how lateralized neural function is linked to lateralized gene activity. A bilaterally symmetric pair of gustatory neurons in the nematode C. elegans, ASEL and ASER, serves as a model to study the genetic basis of functional lateralization as this pair senses a number of chemicals in a left/right asymmetric manner. The extent of functional lateralization of the ASE neurons and genes responsible for the left/right asymmetric activity of ASEL/R are unknown. We show here that a large panel of salt ions is sensed in a left/right asymmetric manner, as demonstrated by behavioral assays, imaging of neural activity with a genetically encoded calcium sensor and by genetic manipulations that alter the fate of either ASEL or ASER. We show that lateralized salt responses allow the worm to discriminate between distinct salt cues. To identify molecules that may be involved in sensing salt ions and/or transmitting such sensory information, we examined the chemotaxis behavior of animals harboring mutations in eight different receptor-type, transmembrane guanylyl cyclases (encoded by gcy genes), which are expressed in either ASEL (gcy-6, gcy-7, gcy-14), ASER (gcy-1, gcy-4, gcy-5, gcy-22) or ASEL and ASER (gcy-19). Disruption of a ASER-expressed gcy gene, gcy-22, resulted in a broad chemotaxis defect to nearly all salts sensed by ASER, as well as to a left/right-asymmetrically sensed amino acid. In contrast, disruption of other gcy genes resulted in highly salt ion-specific chemosensory defects. Furthermore, we show that not only the cyclase domain, but also the extracellular domain of GCY proteins is important for their activity in salt sensation. Our findings broaden our understanding of lateralities in neural function, provide insights into how this laterality is molecularly encoded and reveal an unusually diverse spectrum of signaling molecules involved in gustatory signal transduction.
登录
查看更多内容
影响因子:
64.8
作者:
Suzuki, Hiroshi;Thiele, Tod R.;Faumont, Serge;Ezcurra, Marina;Lockery, Shawn R.;Schafer, William R.
通讯作者:
Schafer, William R.
DOI:
10.1073/pnas.0610877104
发表时间:
2007-02-13
影响因子:
11.1
作者:
Chelur, Dattananda S.;Chalfie, Martin
通讯作者:
Chalfie, Martin
影响因子:
3.7
作者:
Frokjaer-Jensen, Christian;Ailion, Michael;Lockery, Shawn R.
通讯作者:
Lockery, Shawn R.
影响因子:
9.2
作者:
Law, E;Nuttley, WM;van der Kooy, D
通讯作者:
van der Kooy, D
影响因子:
64.8
作者:
van den Akker, F;Zhang, XL;Yee, VC
通讯作者:
Yee, VC