ArticleThe Journal of cell biology1985
The membrane skeleton of a unicellular organism consists of bridged, articulating strips.
Article in The Journal of cell biology, 1985. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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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Who cites it
5 citing papers in PubMed, 48 citations in OpenAlex.
- Article
- The four-transmembrane protein IP39 of Euglena forms strands by a trimeric unit repeat.Nature communications · 2013Article
- Major epiplasmic proteins of ciliates are articulins: cloning, recombinant expression, and structural characterization.The Journal of cell biology · 1995Article
- The two major membrane skeletal proteins (articulins) of Euglena gracilis define a novel class of cytoskeletal proteins.The Journal of cell biology · 1992Article
- Properties and topography of the major integral plasma membrane protein of a unicellular organism.The Journal of cell biology · 1988Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this paper we show that a membrane skeleton associated with the plasma membrane of the unicellular organism Euglena consists of approximately 40 individual S-shaped strips that overlap along their lateral margins. The region of strip overlap is occupied by a set of microtubule-associated bridges and microtubule-independent bridges. Both cell form and plasma membrane organization are dependent on the integrity of this membrane skeleton. Removal of the membrane skeleton with a low-molar base results in loss of membrane form and randomization of the paracrystalline membrane interior characteristic of untreated cells. Conversely, removal of the plasma membrane and residual cytoplasm with lithium 3,5-diiodosalicylate/Nonidet P-40 yields cell ghosts that retain the form of the original cell but consist only of the membrane skeleton. Two major polypeptides of 86 and 80 KD persist in the skeleton and two other major proteins of 68 and 39 kD are associated with the plasma membrane fraction. None of these components appears to be the same as the major polypeptides (spectrins, band 3) of the erythrocyte ghost, the other cell system in which a well-defined peripheral membrane skeleton has been identified. We suggest that the articulating strips of euglenoids are not only the basic unit of cell and surface form, but that they are also positioned to mediate or accommodate surface movements by sliding, and to permit surface replication by intussusception.
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