منابع مشابه
Big proteins Ran into import difficulties
Calcium increases the appetite eutrophils are gluttonous little cells—they will engulf just about any small particle that comes their way. But eating up an entire bacterium takes significant effort. On page 181, Dewitt and Hallett report that neutrophils need integrins and a Ca 2 ϩ boost to build a mouth that is up to the task. Phagocytosis around a particle occurs in a series of steps that inc...
متن کاملCOMMENTARY Import of proteins into chloroplasts
Chloroplasts are the sites of photosynthesis in eukaryotic plants and are able to harvest solar energy for the synthesis of carbon skeletons. They, like mitochondria, are enclosed by two membranes; the outer and the inner envelope. The latter is the actual permeability barrier between the cytosol and the chloroplast stroma and the site of different metabolite translocators that coordinate the m...
متن کاملImport of proteins into the peroxisomal matrix
Peroxisomes constitute a dynamic compartment in all nucleated cells. They fulfill diverse metabolic tasks in response to environmental changes and cellular demands. This adaptation is implemented by modulation of the enzyme content of the organelles, which is accomplished by dynamically operating peroxisomal protein transport machineries. Soluble import receptors recognize their newly synthesiz...
متن کاملImport of proteins into the chloroplast lumen.
Plastocyanin is a nuclear-encoded protein that is functional in the thylakoid lumen of the chloroplast. It is synthesized in the cytoplasm as a precursor with an N-terminal transit peptide of 66 amino acids. Its transport route involves two steps, import into the chloroplasts and subsequent routing over the thylakoid membrane into the lumen. Concomitant with the transport, the transit peptide i...
متن کاملNTF2 mediates nuclear import of Ran.
Importin beta family transport receptors shuttle between the nucleus and the cytoplasm and mediate transport of macromolecules through nuclear pore complexes (NPCs). The interactions between these receptors and their cargoes are regulated by binding RanGTP; all receptors probably exit the nucleus complexed with RanGTP, and so should deplete RanGTP continuously from the nucleus. We describe here...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 2002
ISSN: 1540-8140,0021-9525
DOI: 10.1083/jcb1591iti3