Basolateral Sorting of the HIV Type 2 and SIV Envelope Glycoproteins in Polarized Epithelial Cells: Role of the Cytoplasmic Domain

1997 ◽  
Vol 13 (8) ◽  
pp. 665-675 ◽  
Author(s):  
JUDITH M. BALL ◽  
MARK J. MULLIGAN ◽  
RICHARD W. COMPANS
Keyword(s):  
Epithelial Cells ◽  
Cytoplasmic Domain ◽  
Envelope Glycoproteins ◽  
Polarized Epithelial Cells

scholarly journals The MAL Protein, an Integral Component of Specialized Membranes, in Normal Cells and Cancer

Cells ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 1065
Author(s):  
Armando Rubio-Ramos ◽  
Leticia Labat-de-Hoz ◽  
Isabel Correas ◽  
Miguel A. Alonso
Keyword(s):  
Epithelial Cells ◽  
Large Body ◽  
Original Description ◽  
Cell Types ◽  
Future Research ◽  
Transmembrane Segments ◽  
Epsilon Toxin ◽  
Proteolipid Proteins ◽  
Polarized Epithelial Cells

The MAL gene encodes a 17-kDa protein containing four putative transmembrane segments whose expression is restricted to human T cells, polarized epithelial cells and myelin-forming cells. The MAL protein has two unusual biochemical features. First, it has lipid-like properties that qualify it as a member of the group of proteolipid proteins. Second, it partitions selectively into detergent-insoluble membranes, which are known to be enriched in condensed cell membranes, consistent with MAL being distributed in highly ordered membranes in the cell. Since its original description more than thirty years ago, a large body of evidence has accumulated supporting a role of MAL in specialized membranes in all the cell types in which it is expressed. Here, we review the structure, expression and biochemical characteristics of MAL, and discuss the association of MAL with raft membranes and the function of MAL in polarized epithelial cells, T lymphocytes, and myelin-forming cells. The evidence that MAL is a putative receptor of the epsilon toxin of Clostridium perfringens, the expression of MAL in lymphomas, the hypermethylation of the MAL gene and subsequent loss of MAL expression in carcinomas are also presented. We propose a model of MAL as the organizer of specialized condensed membranes to make them functional, discuss the role of MAL as a tumor suppressor in carcinomas, consider its potential use as a cancer biomarker, and summarize the directions for future research.

scholarly journals Efficient formation of bipolar microtubule bundles requires microtubule-bound γ-tubulin complexes

2005 ◽  
Vol 169 (2) ◽  
pp. 297-308 ◽  
Author(s):  
Marcel E. Janson ◽  
Thanuja Gangi Setty ◽  
Anne Paoletti ◽  
P.T. Tran
Keyword(s):  
Epithelial Cells ◽  
Fission Yeast ◽  
Linear Array ◽  
Spatial Separation ◽  
Wild Type ◽  
Basic Form ◽  
Yeast Protein ◽  
Polarized Epithelial Cells ◽  
In Cells

The mechanism for forming linear microtubule (MT) arrays in cells such as neurons, polarized epithelial cells, and myotubes is not well understood. A simpler bipolar linear array is the fission yeast interphase MT bundle, which in its basic form contains two MTs that are bundled at their minus ends. Here, we characterize mto2p as a novel fission yeast protein required for MT nucleation from noncentrosomal γ-tubulin complexes (γ-TuCs). In interphase mto2Δ cells, MT nucleation was strongly inhibited, and MT bundling occurred infrequently and only when two MTs met by chance in the cytoplasm. In wild-type 2, we observed MT nucleation from γ-TuCs bound along the length of existing MTs. We propose a model on how these nucleation events can more efficiently drive the formation of bipolar MT bundles in interphase. Key to the model is our observation of selective antiparallel binding of MTs, which can both explain the generation and spatial separation of multiple bipolar bundles.

Role Of The Type 2 Alveolar Epithelial Cells In An Experimental Model Of Acute Lung Injury

2012 ◽  
Author(s):  
Sonia Garcia-Hernandez ◽  
Ricardo Gutierrez ◽  
Lucio Diaz-Flores ◽  
Jesus Villar ◽  
Francisco Valladares
Keyword(s):  
Acute Lung Injury ◽  
Epithelial Cells ◽  
Lung Injury ◽  
Experimental Model ◽  
Alveolar Epithelial Cells ◽  
Alveolar Epithelial

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.

scholarly journals Alveolar macrophages and epithelial cells: The art of living together

2021 ◽  
Vol 218 (10) ◽  
Author(s):  
Derek Clements ◽  
Juliana Idoyaga
Keyword(s):  
Epithelial Cells ◽  
Alveolar Macrophages ◽  
Alveolar Epithelial Cells ◽  
Art Of Living ◽  
Alveolar Epithelial ◽  
Living Together

In this issue of JEM, Gschwend et al. (2021. J. Exp. Med.https://doi.org/10.1084/jem.20210745) reveal the indispensable role of alveolar epithelial cells type 2 in controlling the density of alveolar macrophages. This study highlights the intricate crosstalk that lung stroma and macrophages undergo to maintain homeostasis.

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