Results 221 to 230 of about 4,545,906 (256)

Interaction of Tyrosine-Based Sorting Signals with Clathrin-Associated Proteins

Science, 1995
Tyrosine-based signals within the cytoplasmic domain of integral membrane proteins mediate clathrin-dependent protein sorting in the endocytic and secretory pathways. A yeast two-hybrid system was used to identify proteins that bind to tyrosine-based signals.
H, Ohno, J, Stewart, M C, Fournier, H, Bosshart, I, Rhee, S, Miyatake, T, Saito, A, Gallusser, T, Kirchhausen, J S, Bonifacino   +9 more
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Intracellular sorting and targeting of melanosomal membrane proteins: identification of signals for sorting of the human brown locus protein, gp75. [PDF]

Journal of Cell Biology, 1995
The structural and functional integrity of cytoplasmic organelles is maintained by intracellular mechanisms that sort and target newly synthesized proteins to their appropriate cellular locations. In melanocytic cells, melanin pigment is synthesized in specialized organelles, melanosomes.
S, Vijayasaradhi, Y, Xu, B, Bouchard, A N, Houghton   +3 more
exaly   +3 more sources

Signal Sorting by G-Protein-Linked Receptors

1995
Publisher Summary The vast range of individual gene products encoding G-protein-linked receptors and the fact that individual neurotransmitters and hormones have, in many cases, the potential to activate multiple receptor subtypes provide the potential for exquisite control of the sensitivity of cellular response to these agents.
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Protein Sorting Signals for Maintaining Transmembrane Proteins in the Endoplasmatic Reticulum

1994
Trafficking and sorting of proteins through the central organellar system has been a focus of interst since Palade (1975) and co-workers formulated the general outline of the secretory pathway. The basics of this pathway are now well established. Nascent proteins are targeted to the first organelle of this pathway, the endoplasmic reticulum, via a ...
M. R. Jackson, P. A. Peterson
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Evolution of Protein Sorting Signals

1997
Sorting signals route proteins to the correct subcellular compartment and define classes of evolutionarily conserved protein motifs. Their surprisingly low degree of sequence conservation suggests that partially functional sorting signals may arise continuously during evolution, and thus that existing proteins may be continually tested in new ...
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Protein sorting signals: Simple peptides with complex functions

1995
Protein sorting signals provide good examples of peptides that can be studied both from a chemical and a biochemical perspective. Their simple designs and low degree of sequence conservation suggest that they are involved in rather non-specific peptide-lipid interactions, yet their ability to discriminate efficiently between the import machineries of ...
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Targeting signals required for protein sorting to sub-chloroplast compartments

Plant Cell Reports
Chloroplasts, distinctive subcellular organelles found exclusively in plant species, contain three membranes: the outer, inner, and thylakoid membranes. They also have three soluble compartments: the intermembrane space, stroma, and thylakoid lumen. Accordingly, delicate sorting mechanisms are required to ensure proper protein targeting to these sub ...
Ji Hyun Kang, Dong Wook Lee
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Mitochondrial protein import in plants – Signals, Sorting, Targeting, Processing and Regulation

Plant Molecular Biology, 1998
Mitochondrial biogenesis requires a coordinated expression of both the nuclear and the organellar genomes and specific intracellular protein trafficking, processing and assembly machinery. Most mitochondrial proteins are synthesised as precursor proteins containing an N-terminal extension which functions as a targeting signal, which is proteolytically ...
E, Glaser, S, Sjöling, M, Tanudji, J, Whelan   +3 more
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Using sorting signals to retain proteins in endoplasmic reticulum

2000
Publisher Summary This chapter describes the use of sorting signals to retain proteins in endoplasmic reticulum. It is desirable to express an altered form of a secreted or membrane protein such that it remains in the endoplasmic reticulum (ER). This approach can be used to accumulate high levels of a particular protein, to test whether the location ...
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SIGNAL-MEDIATED SORTING OF MEMBRANE PROTEINS BETWEEN THE ENDOPLASMIC RETICULUM AND THE GOLGI APPARATUS

Annual Review of Cell and Developmental Biology, 1996
Each organelle of the secretory pathway is required to selectively allow transit of newly synthesized secretory and plasma membrane proteins and also to maintain a unique set of resident proteins that define its structural and functional properties.
Teasdale, RD, Jackson, MR
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