Document Detail

Knockdown of p180 eliminates the terminal differentiation of a secretory cell line.
MedLine Citation:
PMID:  19037105     Owner:  NLM     Status:  MEDLINE    
We have previously reported that the expression in yeast of an integral membrane protein (p180) of the endoplasmic reticulum (ER), isolated for its ability to mediate ribosome binding, is capable of inducing new membrane biogenesis and an increase in secretory capacity. To demonstrate that p180 is necessary and sufficient for terminal differentiation and acquisition of a secretory phenotype in mammalian cells, we studied the differentiation of a secretory cell line where p180 levels had been significantly reduced using RNAi technology and by transiently expressing p180 in nonsecretory cells. A human monocytic (THP-1) cell line, that can acquire macrophage-like properties, failed to proliferate rough ER when p180 levels were lowered. The Golgi compartment and the secretion of apolipoprotein E (Apo E) were dramatically affected in cells expressing reduced p180 levels. On the other hand, expression of p180 in a human embryonic kidney nonsecretory cell line (HEK293) showed a significant increase in proliferation of rough ER membranes and Golgi complexes. The results obtained from knockdown and overexpression experiments demonstrate that p180 is both necessary and sufficient to induce a secretory phenotype in mammalian cells. These findings support a central role for p180 in the terminal differentiation of secretory cells and tissues.
Payam Benyamini; Paul Webster; David I Meyer
Related Documents :
15529755 - Hydrostatic pressure induced death of mammalian cells engages pathways related to apopt...
12069805 - Sphingosine-1-phosphate and lipid phosphohydrolases.
11929515 - Inla- but not inlb-mediated internalization of listeria monocytogenes by non-phagocytic...
12356725 - Quantitative proteomic analysis of myc oncoprotein function.
18670645 - Bh3 mimetics reactivate autophagic cell death in anoxia-resistant malignant glioma cells.
23614455 - Efficient cell and cell-sheet harvesting based on smart surfaces coated with a multifun...
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2008-11-26
Journal Detail:
Title:  Molecular biology of the cell     Volume:  20     ISSN:  1939-4586     ISO Abbreviation:  Mol. Biol. Cell     Publication Date:  2009 Jan 
Date Detail:
Created Date:  2009-01-15     Completed Date:  2009-03-12     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  9201390     Medline TA:  Mol Biol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  732-44     Citation Subset:  IM    
Department of Biological Chemistry, The David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Calnexin / metabolism
Cell Differentiation / physiology*
Cell Line / physiology
Endoplasmic Reticulum / metabolism,  ultrastructure
Golgi Apparatus / metabolism,  ultrastructure
Monocytes / physiology,  ultrastructure
RNA Interference
Receptors, Cytoplasmic and Nuclear / genetics,  metabolism*
Secretory Pathway / physiology*
Grant Support
P-30 DC006276-03/DC/NIDCD NIH HHS; R-01 GM-38538/GM/NIGMS NIH HHS
Reg. No./Substance:
0/Receptors, Cytoplasmic and Nuclear; 0/ribosome receptor p180, human; 139873-08-8/Calnexin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  The Aspergillus nidulans kinesin-3 UncA motor moves vesicles along a subpopulation of microtubules.
Next Document:  SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and enhancing FOXO1's repressive i...