The road not taken: Less traveled roads from the TGN to the plasma membrane [PDF]
, 2015 : The trans-Golgi network functions in the distribution of cargo into different transport vesicles that are destined to endosomes, lysosomes and the plasma membrane. Over the years, it has become clear that more than one transport pathway promotes plasma
Anne Spang, Spang, Anne
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An N‐terminal hydrophobic peak is the sorting signal of regulated secretory proteins [PDF]
FEBS Letters, 1995 Endocrine and exocrine cells each contain a regulated and constitutive secretory pathway. The presence of two distinct secretory pathways in the same cell type requires a sorting step to direct secretory proteins to the correct pathway. It is thought that regulated secretory proteins contain a specific sorting signal.
Gorr, Sven-Ulrik, Darling, Douglas S.
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Regulation of Notch Endosomal Sorting and Signaling by Drosophila Nedd4 Family Proteins [PDF]
Current Biology, 2004 The Notch receptor mediates a short-range signal that regulates many cell fate decisions. The misregulation of Notch has been linked to cancer and to developmental disorders. Upon binding to its ligands, Delta (Dl) or Serrate (Ser), the Notch ectodomain is shed by the action of an ADAM protease.
Wilkin, M B +9 more
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Rsp5 Ubiquitin Ligase Is Required for Protein Trafficking in Saccharomyces cerevisiae COPI Mutants [PDF]
, 2012 Retrograde trafficking from the Golgi to the endoplasmic reticulum (ER) depends on the formation of vesicles coated with the multiprotein complex COPI.
Joanna Kaminska +7 more
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Vesicular traffic in polarized epithelial cells : identification and characterization of general and epithelial specific factors [PDF]
, 1994 Polarized epithelial cells are differentiated into apical and basolateral plasma membrane domains separated by tight junctions. The apical cell surface usually faces the external milieu, the basolateral domain provides cell-cell and cell-substratum ...
Fiedler, Klaus
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Characterization of granule-like structures in non-endocrine cells [PDF]
, 2006 All eukaryotic cells have transport pathways to constitutively secrete proteins. Endocrine, neuroendocrine, and exocrine cells in addition have a regulated secretory pathway that serves the controlled release of hormones, neuropeptides or digestive ...
Stettler, Hansruedi
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Sorting and Targeting of Melanosomal Membrane Proteins: Signals, Pathways, and Mechanisms [PDF]
Pigment Cell Research, 2000 Newly synthesized melanosomal proteins, like many other cellular proteins, traverse through a series of intracellular compartments en route to melanosomes. Entry and exit of proteins through these compartments is orchestrated by cellular sorting machinery that recognize specific sorting signals.
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Characterization of Sorting Signals in the β-Amyloid Precursor Protein Cytoplasmic Domain [PDF]
Journal of Biological Chemistry, 1995 The beta-amyloid precursor protein (APP) is proteolytically processed to generate beta-amyloid protein, the principal protein component of neuropathological lesions characteristic of Alzheimer's disease. To investigate potential sorting signals in the cytoplasmic tail of APP, we transplanted APP cytoplasmic tail sequences into the cytoplasmic tail of ...
A, Lai, S S, Sisodia, I S, Trowbridge
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Reprogramming Hansenula polymorpha for penicillin production: expression of the Penicillium chrysogenum pcl gene [PDF]
, 2007 We aim to introduce the penicillin biosynthetic pathway into the methylotrophic yeast Hansenula polymorpha. To allow simultaneous expression of the multiple genes of the penicillin biosynthetic pathway, additional markers were required.
Ida J. van der Klei +12 more
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Cell wall sorting signals in surface proteins of gram‐positive bacteria. [PDF]
The EMBO Journal, 1993 Staphylococcal protein A is anchored to the cell wall, a unique cellular compartment of Gram-positive bacteria. The sorting signal sufficient for cell wall anchoring consists of an LPXTG motif, a C-terminal hydrophobic domain and a charged tail. Homologous sequences are found in many surface proteins of Gram-positive bacteria and we explored the ...
O, Schneewind +2 more
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