Interaction of FUN14 domain containing 1, a mitochondrial outer membrane protein, with kinesin light chain 1 via the tetratricopeptide repeat domain
نویسندگان
چکیده
منابع مشابه
Hybrid Sterility in Rice (Oryza sativa L.) Involves the Tetratricopeptide Repeat Domain Containing Protein.
Intersubspecific hybrid sterility is a common form of reproductive isolation in rice (Oryza sativa L.), which significantly hampers the utilization of heterosis between indica and japonica varieties. Here, we elucidated the mechanism of S7, which specially causes Aus-japonica/indica hybrid female sterility, through cytological and genetic analysis, map-based cloning, and transformation experime...
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The molecular interplay between cargo recognition and regulation of the activity of the kinesin-1 microtubule motor is not well understood. Using the lysosome adaptor SKIP (also known as PLEKHM2) as model cargo, we show that the kinesin heavy chains (KHCs), in addition to the kinesin light chains (KLCs), can recognize tryptophan-acidic-binding determinants on the cargo when presented in the con...
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Objective: The purpose of this study was to measure the changes of the SUN1 protein levels on soleus muscle in diabetic male wistar rats. Materials and Methods: Twenty male Wistar rats with 10 weeks old and weighing 200-250 grams were selected. After two weeks, the rats were divided into two groups (diabetic group and healthy group). After 12 hours fasting, diabetes was induced by intraperiton...
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Pentatricopeptide repeat domain protein 1 lowers the levels of mitochondrial leucine tRNAs in cells
Although the basic components and mechanisms of mitochondrial transcription in mammals have been described, the components involved in mRNA processing, translation and stability remain largely unknown. In plants, pentatricopeptide domain RNA-binding proteins regulate the stability, expression and translation of mitochondrial transcripts; therefore, we investigated the role of an uncharacterized...
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ژورنال
عنوان ژورنال: Biomedical Reports
سال: 2016
ISSN: 2049-9434,2049-9442
DOI: 10.3892/br.2016.818