ArticleCommunicative & integrative biology2017
Sequence and biochemical analysis of Arabidopsis SP1 protein, a regulator of organelle biogenesis.
Article in Communicative & integrative biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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4 citing papers in PubMed, 8 citations in OpenAlex.
- Genome landscape of the universal stress protein gene family in lettuce and expression profile in response to heat stress.BMC plant biology · 2025Article
- Mitochondrial proteases and their roles in mitophagy in plants, animals, and yeast.Plant & cell physiology · 2025Review
- In silico identification and functional annotation of universal stress protein (USP) gene family in Chenopodium quinoa.Scientific reports · 2025Article
- Multiple ubiquitin E3 ligase genes antagonistically regulate chloroplast-associated protein degradation.Current biology : CB · 2023Article
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2 authors at 1 institution in 1 country.
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Abstract
Peroxisomes, chloroplasts, and mitochondria are essential eukaryotic organelles that host a suite of metabolic processes crucial to energy metabolism and development. Regulatory mechanisms of the dynamics and biogenesis of these important organelles have begun to be discovered in plants. We recently showed that, aside from its previously reported role in targeting chloroplast protein import proteins, the Arabidopsis ubiquitin E3 ligase SP1 (suppressor of ppi1 locus1) negatively regulates peroxisome matrix protein import by promoting the ubiquitination and destabilization of PEX13 and possibly PEX14 and other components of the peroxisome protein import apparatus. Here, we compared protein sequence and domain structure of SP1-like proteins in Arabidopsis and their human homolog, Mitochondrial-Anchored Protein Ligase (MAPL). We further characterized SP1 protein in respect to its membrane topology and ubiquitin E3 ligase activity.
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