The lateral mobility of NHE3 on the apical membrane of polarized epithelial cells is limited by binding to PDZ domain proteins NHERF1/2 as determined by fluorescence recovery after photobleaching (FRAP)

2003 ◽  
Vol 124 (4) ◽  
pp. A472
Author(s):  
Boyoung Cha ◽  
Michael Edidin ◽  
Anne K. Kenworthy ◽  
Mark Donowitz
Keyword(s):  
Epithelial Cells ◽  
Fluorescence Recovery After Photobleaching ◽  
Apical Membrane ◽  
Pdz Domain ◽  
Fluorescence Recovery ◽  
Lateral Mobility ◽  
Pdz Domain Proteins ◽  
Polarized Epithelial Cells

scholarly journals Sorting of Marburg Virus Surface Protein and Virus Release Take Place at Opposite Surfaces of Infected Polarized Epithelial Cells

2001 ◽  
Vol 75 (3) ◽  
pp. 1274-1283 ◽  
Author(s):  
Christian Sänger ◽  
Elke Mühlberger ◽  
Elena Ryabchikova ◽  
Larissa Kolesnikova ◽  
Hans-Dieter Klenk ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Apical Membrane ◽  
Basolateral Membrane ◽  
Surface Protein ◽  
Hemorrhagic Fever ◽  
Marburg Virus ◽  
Virus Surface ◽  
Mdckii Cells ◽  
Vesicular Stomatitis ◽  
Polarized Epithelial Cells

ABSTRACT Marburg virus, a filovirus, causes severe hemorrhagic fever with hitherto poorly understood molecular pathogenesis. We have investigated here the vectorial transport of the surface protein GP of Marburg virus in polarized epithelial cells. To this end, we established an MDCKII cell line that was able to express GP permanently (MDCK-GP). The functional integrity of GP expressed in these cells was analyzed using vesicular stomatitis virus pseudotypes. Further experiments revealed that GP is transported in MDCK-GP cells mainly to the apical membrane and is released exclusively into the culture medium facing the apical membrane. When MDCKII cells were infected with Marburg virus, the majority of GP was also transported to the apical membrane, suggesting that the protein contains an autonomous apical transport signal. Release of infectious progeny virions, however, took place exclusively at the basolateral membrane of the cells. Thus, vectorial budding of Marburg virus is presumably determined by factors other than the surface protein.

scholarly journals Move your microvilli

2014 ◽  
Vol 207 (1) ◽  
pp. 9-11 ◽  
Author(s):  
Robert S. Fischer
Keyword(s):  
Wound Healing ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Cell Polarity ◽  
Apical Membrane ◽  
Apical Surface ◽  
Epithelial Cell Polarity ◽  
Cell Biol ◽  
Polarized Epithelial Cells

Polarized epithelial cells create tightly packed arrays of microvilli in their apical membrane, but the fate of these microvilli is relatively unknown when epithelial cell polarity is lost during wound healing. In this issue, Klingner et al. (2014. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201402037) show that, when epithelial cells become subconfluent, actomyosin contractions locally within the apical cortex cause their microvilli to become motile over the dorsal/apical surface. Their unexpected observations may have implications for epithelial responses in wound healing and disease.

scholarly journals Human Respiratory Syncytial Virus Glycoproteins Are Not Required for Apical Targeting and Release from Polarized Epithelial Cells

2008 ◽  
Vol 82 (17) ◽  
pp. 8664-8672 ◽  
Author(s):  
Melissa Batonick ◽  
Antonius G. P. Oomens ◽  
Gail W. Wertz
Keyword(s):  
Respiratory Syncytial Virus ◽  
Epithelial Cells ◽  
Apical Membrane ◽  
Human Respiratory Syncytial Virus ◽  
Viral Gene ◽  
Recombinant Viruses ◽  
Intracellular Targeting ◽  
Polarized Epithelial Cells ◽  
Syncytial Virus ◽  
Apical Sorting

ABSTRACT Human respiratory syncytial virus (HRSV) is released from the apical membrane of polarized epithelial cells. However, little is known about the processes of assembly and release of HRSV and which viral gene products are involved in the directional maturation of the virus. Based on previous studies showing that the fusion (F) glycoprotein contained an intrinsic apical sorting signal and that N- and O-linked glycans can act as apical targeting signals, we investigated whether the glycoproteins of HRSV were involved in its directional targeting and release. We generated recombinant viruses with each of the three glycoprotein genes deleted individually or in groups. Each deleted gene was replaced with a reporter gene to maintain wild-type levels of gene expression. The effects of deleting the glycoprotein genes on apical maturation and on targeting of individual proteins in polarized epithelial cells were examined by using biological, biochemical, and microscopic assays. The results of these studies showed that the HRSV glycoproteins are not required for apical maturation or release of the virus. Further, deletion of one or more of the glycoprotein genes did not affect the intracellular targeting of the remaining viral glycoproteins or the nucleocapsid protein to the apical membrane.

scholarly journals A Regulated Complex of the Scaffolding Proteins PDZK1 and EBP50 with Ezrin Contribute to Microvillar Organization

2010 ◽  
Vol 21 (9) ◽  
pp. 1519-1529 ◽  
Author(s):  
David P. LaLonde ◽  
Damien Garbett ◽  
Anthony Bretscher
Keyword(s):  
Epithelial Cells ◽  
Complex Formation ◽  
Ternary Complex ◽  
Apical Membrane ◽  
Pdz Domain ◽  
Scaffolding Proteins ◽  
Pdz Domains ◽  
Zona Occludens

PDZK1 and ezrin, radixin, moesin binding phosphoprotein 50 kDa (EBP50) are postsynaptic density 95/disc-large/zona occludens (PDZ)-domain–containing scaffolding proteins found in the apical microvilli of polarized epithelial cells. Binary interactions have been shown between the tail of PDZK1 and the PDZ domains of EBP50, as well as between EBP50 and the membrane–cytoskeletal linking protein ezrin. Here, we show that these molecules form a regulated ternary complex in vitro and in vivo. Complex formation is cooperative because ezrin positively influences the PDZK1/EBP50 interaction. Moreover, the interaction of PDZK1 with EBP50 is enhanced by the occupancy of EBP50's adjacent PDZ domain. The complex is further regulated by location, because PDZK1 shuttles from the nucleus in low confluence cells to microvilli in high confluence cells, and this regulates the formation of the PDZK1/EBP50/ezrin complex in vivo. Knockdown of EBP50 decreases the presence of microvilli, a phenotype that can be rescued by EBP50 re-expression or expression of a PDZK1 chimera that is directly targeted to ezrin. Thus, when appropriately located, PDZK1 can provide a function necessary for microvilli formation normally provided by EBP50. By entering into the ternary complex, PDZK1 can both enhance the scaffolding at the apical membrane as well as augment EBP50's role in microvilli formation.

The M3/M4 cytoplasmic loop of the α1 subunit restricts GABAARs lateral mobility: A study using fluorescence recovery after photobleaching

2006 ◽  
Vol 63 (12) ◽  
pp. 747-757 ◽  
Author(s):  
Macarena Perán ◽  
Helen Hooper ◽  
Houria Boulaiz ◽  
Juan A. Marchal ◽  
Antonia Aránega ◽  
...  
Keyword(s):  
Fluorescence Recovery After Photobleaching ◽  
Fluorescence Recovery ◽  
Lateral Mobility ◽  
Cytoplasmic Loop ◽  
Α1 Subunit

scholarly journals Polarized Budding of Measles Virus Is Not Determined by Viral Surface Glycoproteins

1998 ◽  
Vol 72 (6) ◽  
pp. 5276-5278 ◽  
Author(s):  
A. Maisner ◽  
H.-D. Klenk ◽  
G. Herrler
Keyword(s):  
Epithelial Cells ◽  
Measles Virus ◽  
Apical Membrane ◽  
Basolateral Membrane ◽  
Envelope Glycoproteins ◽  
Virus Release ◽  
Membrane Domain ◽  
Polarized Epithelial Cells ◽  
Viral Surface ◽  
Surface Glycoproteins

ABSTRACT For viruses that mature by a budding process, the envelope glycoproteins are considered the major determinants for the site of virus release from polarized epithelial cells. Viruses are usually released from that membrane domain where the viral surface glycoproteins are transported to. We here report that measles virus has developed a different maturation strategy. Measles virus was found to be released from the apical membrane domain of polarized epithelial cells, though the surface glycoproteins H and F were transported in a nonpolarized fashion and to the basolateral membrane domain, respectively.

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