Molecular Cloning of the Zeta Chain of the T Cell Antigen Receptor

Weissman, Allan M.; Baniyash, Michal; Hou, Damon; Samelson, Lawrence E.; Burgess, Wilson H.; Klausner, Richard D.

doi:10.1126/science.3278377

Cited by 262 publications

(119 citation statements)

References 37 publications

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“…4-B with either anti-Vb or anti-CD3e monoclonal antibody after TCR cross linking is within threefold. The extra membrane portion of CD3z has only two accessible residues at the top and the bottom end of the sequence [24]. The change in accessibility of sulfo-NHS-biotin may be most easily explained by conformational change of the molecule, although other possibilities such as the determinant blockade by an unknown CD3 ligand cannot formally be excluded.…”

Section: Discussionmentioning

confidence: 99%

Changes in Arrangement and in Conformation of Molecular Components of Peripheral T‐Cell Antigen Receptor Complex After Ligand Binding: Analyses by Co‐Precipitation Profiles

et al. 1997

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Amounts of co-precipitating CD3 components by anti-T-cell receptor (TCR)Vb or anti-CD4/8 monoclonal antibodies were compared between non-stimulated and stimulated splenic T cells. The amounts of co-precipitating CD3d, e and g chains with TCRab and with CD4/8 were not significantly changed after TCR ligation. The apparent amount of CD3z chain co-precipitated with TCRab increased up to threefold, while the actual amount of co-precipitating CD3z with TCRab and the total amount of specifically precipitated CD3z are not changed after cross linking of TCR. The apparent amount of CD3z chain co-precipitated with CD4/8 also increased. Unlike co-precipitation with TCRab, the actual amount of CD3z co-precipitated with CD4/8 increased significantly. This observation suggests a conformational change as well as the relocation of CD3z molecules within the TCR complex after the signal delivery. After TCR ligation, CD3z chains relocate to the vicinity of either CD4 or CD8 molecules. In addition, when cross linking and binding signals are compared, CD3 chains undergo two distinct phases of conformational change. The early conformational change caused by ligand binding is positively related to the induction of proliferative responses, while the later conformational change caused by the cross linking of TCR does not induce but enhances the proliferative response.

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Section: Discussionmentioning

confidence: 99%

Changes in Arrangement and in Conformation of Molecular Components of Peripheral T‐Cell Antigen Receptor Complex After Ligand Binding: Analyses by Co‐Precipitation Profiles

et al. 1997

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“…(1985) and Weissman et al (1988)). The cysteine (C) residue involved in the dimerization 01 the ~ chain and Ihe aspartic acid (0-) residues lound in the CD3-~ TM segment are indicated.…”

Section: 164 28 29 30mentioning

confidence: 99%

“…In the ~D66-157 moleeule, residues 66-157 have been deleted and replaced by the sequence QACKL (see Experimental Procedures). The CD3-i; residues are numbered according to Weissman et al (1988).…”

Section: 164 28 29 30mentioning

confidence: 99%

The T cell receptor/CD3 complex is composed of at least two autonomous transduction modules

Wegener

Letourneur

Hoeveler

et al. 1992

Cell

415

294

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SummaryReeent studies have demonstrated that the CD3-~ subunlt of the T eell antigen reeeptor (TCR) eomplex Is involved In signal transduetlon. However, the funetlon of the remalnlng Invariant subunits, CD3-y, -ö, and e, Is still poorly understood. To examine thelr role In TCR funetlon, we have eonstrueted TCR/CD3 eomplexes devold of tunetlonal ~ subunlt and showed that they are still able to trigger the produellon of Interleukln-2 in response to antigen or superantigen. These data, together with previous results, Indleate that the TCR/ CD3 eomplex Is eomposed of at least two parallel Iransduelng unlts, made 01 the YÖE and ~ ehalns, respeetlvely, Furthermore, the analysis 01 partially truneated ~ ehains has led us to Indlvlduallze a lunetlonal domaln that may have eonstltuted the buildlng block of most of the transduelng subunlts assoelated wlth antigen reeeptors and some Fe receptors. IntroduetionThe T cell antigen receptor (TCR) is a multisubunit complex composed of the products of at least six distinct genes. The TCR a and TCR ß subunits exist as disulfidelinked heterodimers, possess short cytoplasmic tails, and contain clonally variable regions that determine the antigenic specificity of the complex. The remaining subunits, termed CD3-y, -ö, -E, -~, and -1], are invariant, noncovalently associated with the TCR aß dimer, and possess large intracytoplasmic domains thought to be responsible for coupling antigen recognition to various signal transductlon pathways. The evolutionarily related y, Ö, and e subunits are expressed as noncovalently associated ye and OE pairs (Koning et al., 1990;Blumberg et al. , 1990; De la Herra et al. , 1991), and display immunoglobulin-like extracellular domains (Gold et al., 1987). In contrast, the ~ and 1] subunlts contaln an extracellular domain of only 9 residues and constitute the prototype of a new protein family that includes the y chain of the high affinity IgE receptor (FceRI)

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“…Three DNA preparations (T-DNA for total mononucleosome preparation, IP-DNA for immunoprecipitate, and S-DNA for supernatant) were blotted to nylon membranes and probed with the following probes: 1) mouse high C o t-1 DNA (Life Technologies); 2) mouse repetitive B1 element-containing plasmid derived from the ␣-fetoprotein gene (11); and 3) a sequence specific to the T-cell receptor gene (12). DNA was labeled by T7 QuickPrime random-priming kit (Amersham Pharmacia Biotech) and hybridized as described below.…”

Section: Immunoprecipitation Of Hmg-nucleosome Complexes and Slot-blomentioning

confidence: 99%

Targeting of High Mobility Group-14/-17 Proteins in Chromatin Is Independent of DNA Sequence

Shirakawa

Herrera

Bustin

et al. 2000

Journal of Biological Chemistry

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Chromosomal proteins high mobility group (HMG)-14 and HMG-17 are nucleosomal-binding proteins that unfold the chromatin fiber and enhance transcription from chromatin templates. Their intracellular organization is dynamic and related to both cell cycle and transcription. Here we examine possible mechanisms for targeting HMG-14/-17 to specific regions in chromatin. Chromatin immunoprecipitation assays indicate that HMG-17 protein is not preferentially associated with chromatin regions containing transcriptionally active genes, or any type of specific DNA. We used a modification of the random amplified polymorphic DNA method to analyze DNA in various HMG-14/-17⅐nucleosome complexes. We found that although HMG-14 or HMG-17 proteins preferentially associate with core particles in which the DNA has a low frequency of CG dinucleotides, the genome does not contain consensus sequences that serve as specific targeting sites for the binding of either HMG-14 or HMG-17 proteins to nucleosomes. We used size exclusion and ion exchange chromatography to demonstrate that nuclei contain a large portion of HMG-17 associated with other proteins in a multiprotein complex. We suggest that these complexes regulate the dynamic organization of HMG-14/-17 in the nucleus and serve to target the proteins to specific sites in chromatin.

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Molecular Cloning of the Zeta Chain of the T Cell Antigen Receptor

Cited by 262 publications

References 37 publications

Changes in Arrangement and in Conformation of Molecular Components of Peripheral T‐Cell Antigen Receptor Complex After Ligand Binding: Analyses by Co‐Precipitation Profiles

Changes in Arrangement and in Conformation of Molecular Components of Peripheral T‐Cell Antigen Receptor Complex After Ligand Binding: Analyses by Co‐Precipitation Profiles

The T cell receptor/CD3 complex is composed of at least two autonomous transduction modules

Targeting of High Mobility Group-14/-17 Proteins in Chromatin Is Independent of DNA Sequence

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