• Proceedings of the Zoological Society Korea Conference
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• 2003.08a
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• pp.196.1-196
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• 2003

No Abstract, See Full Text

• The Korean Journal of Zoology
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• v.38 no.2
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• pp.220-229
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• 1995

uftraspirocle (usa) gene product (Uspl is a member of the superfamilv of steroid hormone receptors in Drosophila melonogaster which mediate the hormone action by heteromerization with ecdvsone receptor (EcR). Based on the genetic and molecular characterization of usp, it has been proposed that Usp funtions in at least three significant developmental pathway: embrvogenesis, eve morphogenesis, and female reproduction. In this study, the expression patterns of Usp were investigated by immunohistochemistrv in individual tissues from diHernt developmental stases of Drosophila. Usp is localized in the nucleus with ubiquitous distribution throughout development. Usp expression is detected throughout embrvogenesis. Usp is expressed in imaginal and lanral tissues from late third instar 18nra. The expression pattern of Usp is overlapped by those of EcR. Also Usp is expressed in differentiating adult reproductive organs. This result suggests that Usp is not a transcriptional regulatory factor modulating hormonal response during development, but also play some roles in female and male reproduction of Drosophila.

• BMB Reports
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• v.48 no.1
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• pp.1-5
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• 2015

Transient Receptor Potential, Melastatin-related, member 4 (TRPM4) channels are $Ca^{2+}$-activated $Ca^{2+}$-impermeable cation channels. These channels are expressed in various types of mammalian tissues including the brain and are implicated in many diverse physiological and pathophysiological conditions. In the past several years, the trafficking processes and regulatory mechanism of these channels and their interacting proteins have been uncovered. Here in this minireview, we summarize the current understanding of the trafficking mechanism of TRPM4 channels on the plasma membrane as well as heteromeric complex formation via protein interactions. We also describe physiological implications of protein-TRPM4 interactions and suggest TRPM4 channels as therapeutic targets in many related diseases.