scholarly journals PDZ-domain-directed basolateral targeting of the peripheral membrane protein FRMPD2 in epithelial cells

2009 ◽  
Vol 122 (18) ◽  
pp. 3374-3384 ◽  
Author(s):  
N. Stenzel ◽  
C. P. Fetzer ◽  
R. Heumann ◽  
K. S. Erdmann
Keyword(s):  
Epithelial Cells ◽  
Membrane Protein ◽  
Pdz Domain ◽  
Peripheral Membrane Protein ◽  
Basolateral Targeting

scholarly journals Identification of the basolateral targeting determinant of a peripheral membrane protein, MacMARCKS, in polarized cells

1998 ◽  
Vol 8 (12) ◽  
pp. 677-683 ◽  
Author(s):  
Monn Monn Myat ◽  
Sandy Chang ◽  
Enrique Rodriguez-Boulan ◽  
Alan Aderem
Keyword(s):  
Membrane Protein ◽  
Polarized Cells ◽  
Peripheral Membrane Protein ◽  
Basolateral Targeting

scholarly journals Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically oriented peripheral membrane protein.

1993 ◽  
Vol 120 (1) ◽  
pp. 117-127 ◽  
Author(s):  
K R Fath ◽  
D R Burgess
Keyword(s):  
Epithelial Cells ◽  
Membrane Protein ◽  
Actin Filaments ◽  
Equilibrium Density ◽  
Marker Enzyme ◽  
Dependent Manner ◽  
Golgi Membranes ◽  
Myosin I ◽  
Peripheral Membrane Protein

In the intestinal brush border, the mechanoenzyme myosin-I links the microvillus core actin filaments with the plasma membrane. Previous immunolocalization shows that myosin-I is associated with vesicles in mature enterocytes (Drenckhahn, D., and R. Dermietzel. 1988. J. Cell Biol. 107:1037-1048) suggesting a potential role mediating vesicle motility. We now report that myosin-I is associated with Golgi-derived vesicles isolated from cells that are rapidly assembling brush borders in intestinal crypts. Crypt cells were isolated in hyperosmotic buffer, homogenized, and fractionated using differential- and equilibrium-density centrifugation. Fractions containing 50-100-nm vesicles, a similar size to those observed in situ, were identified by EM and were shown to contain myosin-I as demonstrated by immunoblotting and immunolabel negative staining. Galactosyltransferase, a marker enzyme for trans-Golgi membranes was present in these fractions, as was alkaline phosphatase, which is an apical membrane targeted enzyme. Galactosyltransferase was also present in vesicles immuno-purified with antibodies to myosin-I. Villin, a marker for potential contamination from fragmented microvilli, was absent. Myosin-I was found to reside on the vesicle "outer" or cytoplasmic surface for it was accessible to exogenous proteases and intact vesicles could be immunolabeled with myosin-I antibodies in solution. The bound myosin-I could be extracted from the vesicles using NaCl, KI and Na2CO3, suggesting that it is a vesicle peripheral membrane protein. These vesicles were shown to bundle actin filaments in an ATP-dependent manner. These results are consistent with a role for myosin-I as an apically targeted motor for vesicle translocation in epithelial cells.

scholarly journals Pilt, a Novel Peripheral Membrane Protein at Tight Junctions in Epithelial Cells

2001 ◽  
Vol 276 (51) ◽  
pp. 48350-48355 ◽  
Author(s):  
Hiroshi Kawabe ◽  
Hiroyuki Nakanishi ◽  
Masanori Asada ◽  
Atsunori Fukuhara ◽  
Koji Morimoto ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Membrane Protein ◽  
Tight Junctions ◽  
Peripheral Membrane Protein

Tunable Electromechanical Nanopore Trap Reveals Populations of Peripheral Membrane Protein Binding Conformations

ACS Nano ◽  
2020 ◽  
Author(s):  
David P. Hoogerheide ◽  
Tatiana K. Rostovtseva ◽  
Daniel Jacobs ◽  
Philip A. Gurnev ◽  
Sergey M. Bezrukov
Keyword(s):  
Membrane Protein ◽  
Protein Binding ◽  
Peripheral Membrane Protein

scholarly journals Dynamics of the Peripheral Membrane Protein P2 from Human Myelin Measured by Neutron Scattering—A Comparison between Wild-Type Protein and a Hinge Mutant

PLoS ONE ◽  
2015 ◽  
Vol 10 (6) ◽  
pp. e0128954 ◽  
Author(s):  
Saara Laulumaa ◽  
Tuomo Nieminen ◽  
Mari Lehtimäki ◽  
Shweta Aggarwal ◽  
Mikael Simons ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Neutron Scattering ◽  
Wild Type ◽  
Type Protein ◽  
Wild Type Protein ◽  
Peripheral Membrane Protein

scholarly journals A Novel Tetanus Neurotoxin-insensitive Vesicle-associated Membrane Protein in SNARE Complexes of the Apical Plasma Membrane of Epithelial Cells

1998 ◽  
Vol 9 (6) ◽  
pp. 1437-1448 ◽  
Author(s):  
Thierry Galli ◽  
Ahmed Zahraoui ◽  
Vadakkanchery V. Vaidyanathan ◽  
Graça Raposo ◽  
Jian Min Tian ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Epithelial Cells ◽  
Membrane Protein ◽  
Apical Plasma Membrane ◽  
Domain Specific ◽  
Tetanus Neurotoxin ◽  
Synaptic Vesicle Exocytosis ◽  
Clostridial Neurotoxins ◽  
Vesicle Exocytosis ◽  
Syntaxin 3

The importance of soluble N-ethyl maleimide (NEM)-sensitive fusion protein (NSF) attachment protein (SNAP) receptors (SNAREs) in synaptic vesicle exocytosis is well established because it has been demonstrated that clostridial neurotoxins (NTs) proteolyze the vesicle SNAREs (v-SNAREs) vesicle-associated membrane protein (VAMP)/brevins and their partners, the target SNAREs (t-SNAREs) syntaxin 1 and SNAP25. Yet, several exocytotic events, including apical exocytosis in epithelial cells, are insensitive to numerous clostridial NTs, suggesting the presence of SNARE-independent mechanisms of exocytosis. In this study we found that syntaxin 3, SNAP23, and a newly identified VAMP/brevin, tetanus neurotoxin (TeNT)-insensitive VAMP (TI-VAMP), are insensitive to clostridial NTs. In epithelial cells, TI-VAMP–containing vesicles were concentrated in the apical domain, and the protein was detected at the apical plasma membrane by immunogold labeling on ultrathin cryosections. Syntaxin 3 and SNAP23 were codistributed at the apical plasma membrane where they formed NEM-dependent SNARE complexes with TI-VAMP and cellubrevin. We suggest that TI-VAMP, SNAP23, and syntaxin 3 can participate in exocytotic processes at the apical plasma membrane of epithelial cells and, more generally, domain-specific exocytosis in clostridial NT-resistant pathways.

Sign in / Sign up

Export Citation Format

Share Document