Cell Surface Molecule Associated with Lymphocyte Homing Is a Ubiquitinated Branched-Chain Glycoprotein

Siegelman, Mark H.; Bond, M.; Gallatin, W. Michael; John, Tom St.; Smith, Howard R.; Fried, VA; Il, Weissman

doi:10.1126/science.3003913

Cited by 301 publications

(134 citation statements)

References 37 publications

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“…6) is also consistent with even more specific functions during development, such as ubiquitin-mediated modulation of cell differentiation or (and) proliferation. In animals, there have been suggestions of ubiquitin involvement in these functions, based on the observation of polyubiquitin gene activation during programmed cell death (without apparent activation of the cells' heat-shock response [Schwartz et al, 19901) and on the cloning of cell-surface hormone receptors as stable ubiquitin-protein conjugates (Siegelman et al, 1986;Leung et al, 1987).…”

Section: Discussionmentioning

confidence: 99%

Differential Accumulation of Sunflower Tetraubiquitin mRNAs during Zygotic Embryogenesis and Developmental Regulation of Their Heat-Shock Response

Almoguera¹,

Coca²,

Jordano³

1995

Plant Physiol.

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We have isolated and sequenced Ha UbiS, a cDNA for a dryseed-stored mRNA that encodes tetraubiquitin. We have observed differential accumulation of tetraubiquitin mRNAs during sunflower (Helianthus annuus 1.) zygotic embryogenesis. These mRNAs were up-regulated during late embryogenesis and reached higher prevalence in the dry seed, where they were found to be associated mainly with provascular tissue. UbiS mRNA, as confirmed by RNase A protection experiments, accumulated also in response to heat shock, but only in leaves and later during postgerminative development. These novel observations demonstrate expression during seed maturation of specific plant polyubiquitin transcripts and developmental regulation of their heat-shock response. Using ubiquitin antibodies we also detected discrete, seed-specific proteins with distinct temporal expression patterns during zygotic embryogenesis. Some of these patterns were concurrent with UbiS mRNA accumulation in seeds. The most abundant ubiquitin-reacting proteins found in mature seeds were small (16-22 kD) and acidic (isoelectric points of 6.1-7.4). Possible functional implications for UbiS expression elicited from these observations are discussed.

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Section: Discussionmentioning

confidence: 99%

Differential Accumulation of Sunflower Tetraubiquitin mRNAs during Zygotic Embryogenesis and Developmental Regulation of Their Heat-Shock Response

Almoguera¹,

Coca²,

Jordano³

1995

Plant Physiol.

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“…variety of in vivo substrates of the ubiquitin conjugating system have been identified, including histones [10], actin [11], cytlins [12], the tumor suppressor p53 [13,14], MATch2 transcr ption repressor [15], cell surface receptors [16][17][18], c-jun [19] and NF~cB [20]. Some ubiquitin conjugating enzymes are able to transfer ubiquitin to the model substrate histone in vitro without any accessory factors, such as E3s.…”

Section: Introductionmentioning

confidence: 99%

Characterization of functionally independent domains in the human ubiquitin conjugating enzyme UbcH2

et al. 1995

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UbcH2 encodes a human ubiquitin conjugating enzyme (E2) able to conjugate ubiquitin to histone H2A in an E3 independent manner in vitro, which indicates that UbcH2 directly interacts with its substrates. To identify parts of the enzyme that are capable of binding H2A, we expressed several deletion mutants of UbcH2 in E. coli and tested the ability of the affinity purified mutant proteins to ubiquitinate H2A in the presence of bacterial expressed E1 and ubiquitin. With this in vitro assay we identified a C-terminal part of UbcH2 to be important for the interaction with H2A. Transfer of this C-terminal domain to another human E2, which is unable to catalyze ubiquitination of histories, leads to a fully active hybrid human ubiquitin conjugating enzyme capable of H2A ubiquitination. These results demonstrate that UbcH2 consists of two functionally independent domains. A N-terminal core domain with ubiquitin conjugating activity, and a C-terminal domain which interacts with substrate proteins.

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“…In the mouse, a monoclonal antibody, MEL-14 (7), defines the peripheral lymph node homing receptor (LHR) to be a 90-to 95-kDa glycoprotein, gp90MEL-14. The working model of the receptor complex is that of a core protein that is highly glycosylated and apparently conjugated to ubiquitin in isopeptide linkage (8,9). In contrast, a Peyer's patch-specific lymphocyte homing receptor, LPAM-1, has been shown to be an a/P heterodimer closely related to the VLA-4 member of the family of integrins (10,11).…”

mentioning

confidence: 99%

Human homologue of mouse lymph node homing receptor: evolutionary conservation at tandem cell interaction domains.

Siegelman

Weissman

1989

Proc. Natl. Acad. Sci. U.S.A.

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A cDNA clone homologous to the mouse lymph node homing receptor core protein (mLHIR,) CD44/gp9OHS' and, together with mLHRc and two other recently described molecules having a similar domain motif, defines a novel class ofadhesion molecules exhibiting distinct evolutionary features. We propose that hLHRc likely represents the protein core of the human homologne of mLHR, functionally as well as structurally.

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Cell Surface Molecule Associated with Lymphocyte Homing Is a Ubiquitinated Branched-Chain Glycoprotein

Cited by 301 publications

References 37 publications

Differential Accumulation of Sunflower Tetraubiquitin mRNAs during Zygotic Embryogenesis and Developmental Regulation of Their Heat-Shock Response

Differential Accumulation of Sunflower Tetraubiquitin mRNAs during Zygotic Embryogenesis and Developmental Regulation of Their Heat-Shock Response

Characterization of functionally independent domains in the human ubiquitin conjugating enzyme UbcH2

Human homologue of mouse lymph node homing receptor: evolutionary conservation at tandem cell interaction domains.

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