Lyt-2-/Lyt 3- variants of a cloned cytolytic T cell line lack an antigen receptor functional in cytolysis.

Dialynas, Deno P.; Loken, Michael R.; Glasebrook, Andrew L.; Fitch, Frank W.

doi:10.1084/jem.153.3.595

Cited by 72 publications

(26 citation statements)

References 23 publications

(13 reference statements)

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“…It consists of two subunits that can associate as homodimers and heterodimers: the ␣ subunit, which has a C-terminal valine; and the ␤ subunit, which is devoid of this signal (52). CD8␣␤ is the main functional co-receptor, although CD8␣␣ is also expressed at the cell surface and is functional, whereas CD8␤␤ is inactive and retained in the ER (53)(54)(55)(56)(57). The co-expression of CD8␣ relocalizes CD8␤ to the cell surface (57,58).…”

Section: Discussionmentioning

confidence: 99%

GRASP65 and GRASP55 Sequentially Promote the Transport of C-terminal Valine-bearing Cargos to and through the Golgi Complex

D’Angelo

Prencipe

Iodice

et al. 2009

Journal of Biological Chemistry

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The Golgi matrix proteins GRASP65 and GRASP55 have recognized roles in maintaining the architecture of the Golgi complex, in mitotic progression and in unconventional protein secretion whereas, surprisingly, they have been shown to be dispensable for the transport of commonly used reporter cargo proteins along the secretory pathway. However, it is becoming increasingly clear that many trafficking machineries operate in a cargo-specific manner, thus we have investigated whether GRASPs may control the trafficking of selected classes of cargo. We have taken into consideration the C-terminal valine-bearing receptors CD8␣ and Frizzled4 that we show bind directly to the PSD95-DlgA-zo-1 (PDZ) domains of GRASP65 and GRASP55. We demonstrate that both GRASPs are needed sequentially for the efficient transport to and through the Golgi complex of these receptors, thus highlighting a novel role for the GRASPs in membrane trafficking. Our results open new perspectives for our understanding of the regulation of surface expression of a class of membrane proteins, and suggests the causal mechanisms of a dominant form of autosomal human familial exudative vitreoretinopathy that arises from the Frizzled4 mutation involving its C-terminal valine.GRASP65 and GRASP55 were identified in in vitro assays as factors that are required for the stacking of the Golgi cisternae (1, 2). This activity arose as the result of the tethering functions displayed by GRASP65 and GRASP55, through their interactions with their partner proteins GM130 and golgin-45, respectively (2-4). Several other studies have shown more recently that the GRASPs are involved in the maintenance of the structure of the Golgi ribbon in mammal cells during interphase, in controlling the fragmentation of the Golgi complex at the onset of mitosis (5-8), in establishing cell polarity in migrating cells (9), and in the consumption of COPII vesicles and the formation of the cis-Golgi in yeast (10).Although the role of the GRASPs in control of the Golgi complex structure (both in interphase and during mitosis) is well established, their involvement in cargo transport along the secretory pathway is still debated. Indeed, a direct role for GRASPs in cargo transport has so far been established only for the unconventional secretion routes in Dictyostilium and Drosophila (11, 12), whereas they have been shown not to be directly involved in the trafficking of commonly studied reporter cargo proteins along the "conventional" secretory pathway (e.g. the temperature-sensitive (ts-045) mutant of the G protein of vesicular stomatitis virus (VSVG) 2 ) and secretory horseradish peroxidase (5, 6, 13, 14). GRASPs can engage different types of interactions including the ones mediated by their PDZ domains, through which the GRASPs cannot only homodimerize, thus participating in cisternal stacking (15) but can also bind the C-terminal valine motifs (C-TVM) of membrane proteins such as protransforming growth factor ␣ and p24a (16,17).Interestingly a C-terminal valine can behave as "transport sign...

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Section: Discussionmentioning

confidence: 99%

GRASP65 and GRASP55 Sequentially Promote the Transport of C-terminal Valine-bearing Cargos to and through the Golgi Complex

D’Angelo

Prencipe

Iodice

et al. 2009

Journal of Biological Chemistry

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“…The two general approaches for examining this interac tion have been either to look for monoclonal antibodies which bind to the immunizing clone, or alternatively to screen for an effect of the monoclonal antibodies on a functional activity of the T-cell clone. Variant clones lacking Lyt-2 had markedly reduced levels of cytotoxic activity, although this diminished functional activity could be overcome by the addition of lectins (87). However, in a more directed sense, it was hoped that some monoclonal antibodies would be clonally specifi c, and thus might be reactive with the T-cell receptor.…”

Section: Antibodies To Murine T-cell Clonesmentioning

confidence: 99%

T-Lymphocyte Clones

Fathman¹,

Frelinger²

1983

Annu. Rev. Immunol.

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To date, the most successful uses of T-cell clones have been in the demonstration that a single type of cell can perform multiple functions. However, their potential usefulness is enormous, and the study of cell interactions using clonal populations has just begun. The development and study of more cloned populations will surely lead to a clearer analysis of cellular interactions in the immune system. The use of T-cell clones and hybridomas to analyze T-cell receptors and/or factors is well under way, and will continue to be an area of intense investigation. Molecular biologists will undoubtedly make more extensive use of T-cell clones in the future, both as a source of cloning material and as transfection recipients. The most exciting area for development, from a medical point of view, is the potential for use of these cell lines or their products in immunotherapy and in providing a mechanism for specifically modulating the immune response.

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“…Studied by Dialynas et al (1981) showed that Con A mediated antigen nonspecific cytotoxicity by a cloned CTL line is not inhibited by Lyt-2 antibodies. There are several possibilities that may explain the discrepancy between our findings and those of Dialynas et al (1981). 1) Blocking by Lyt-2 antibody may be dependent on the concentration of Con A used.…”

Section: Role Of Lyt-2 Antigens In Ctl-mediated Antigen Non-specific mentioning

confidence: 99%

Molecular Interactions in T‐Cell‐Mediated Cytotoxicity

Bonavida

Bradley

Fan

et al. 1983

Immunological Reviews

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Lyt-2-/Lyt 3- variants of a cloned cytolytic T cell line lack an antigen receptor functional in cytolysis.

Cited by 72 publications

References 23 publications

GRASP65 and GRASP55 Sequentially Promote the Transport of C-terminal Valine-bearing Cargos to and through the Golgi Complex

GRASP65 and GRASP55 Sequentially Promote the Transport of C-terminal Valine-bearing Cargos to and through the Golgi Complex

T-Lymphocyte Clones

Molecular Interactions in T‐Cell‐Mediated Cytotoxicity

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