Binding Constants and Stoichiometries of Glyceraldehyde 3-Phosphate Dehydrogenase-Tubulin Complexes

Muronetz, Vladimir I.; Wang, Zhixin; Keith, Tim J.; Knull, Harvey R.; Srivastava, D. K.

doi:10.1006/abbi.1994.1385

Cited by 61 publications

(34 citation statements)

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“…Each 335-amino acid polypeptide contains two domains: an NAD ϩ binding/Rossmann-fold domain (residues 1-150 and 317-335) and a catalytic domain (residues 151-316). GAPDH is a multifunctional enzyme implicated in a variety of cellular processes including nucleic acid binding (13,(15)(16)(17)(18)(19), DNA replication and repair (20), nuclear tRNA transport (18), apoptosis (21,22), microtubule bundling (23), membrane fusion (24), neurodegenerative disorders (25,26), and heme incorporation (27). The mechanism by which GAPDH switches among these various functions in the cell is unknown but may depend on the cell status and GAPDH posttranslational modifications (for reviews, see Refs.…”

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confidence: 99%

A Dimer Interface Mutation in Glyceraldehyde-3-Phosphate Dehydrogenase Regulates Its Binding to AU-rich RNA

White

Khan

Deredge

et al. 2015

Journal of Biological Chemistry

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Background:The glycolytic enzyme GAPDH is a non-canonical RNA-binding protein.Results: A dimer interface mutation impairs the two-step binding of GAPDH to AU-rich elements from TNF-␣ mRNA and leads to RNA structural changes. Conclusion: Dimer and tetramer interface residues are important for GAPDH-RNA binding. Significance: We propose a novel model for GAPDH binding to AU-rich RNA via the oligomeric interfaces.

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confidence: 99%

A Dimer Interface Mutation in Glyceraldehyde-3-Phosphate Dehydrogenase Regulates Its Binding to AU-rich RNA

White

Khan

Deredge

et al. 2015

Journal of Biological Chemistry

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“…functions identified so far include binding of cytoskeleton organizing proteins such as tubulin (43), actin (44), and ICAM-1 (45), regulation of gene expression by binding of AU-rich 3Ј-untranslated regions of mRNA (46) and specific interaction with parainfluenza and hepatitis A virus RNA (47,48), participation in DNA replication as DNA polymerase ␣-associated, P1,P4-di(adenosine-5Ј)-tetraphosphate-binding protein (49), catalysis of membrane vesicle fusion in endocytosis (50), binding of pathologic neurodegenerative proteins possessing polyglutamine domains such as Huntington and DRPLA (51), participation in DNA repair as uracil DNA glycosylase (52), and modulation of phosphoribulokinase activity in Chlamydomonas chloroplasts (53,54). In the last mentioned, complex formation with GAPDH alters the conformation and catalytic properties of phosphoribulokinase.…”

Section: Figmentioning

confidence: 99%

Glyceraldehyde-3-phosphate Dehydrogenase and Nm23-H1/Nucleoside Diphosphate Kinase A

Engel¹,

Seifert²,

Theisinger³

et al. 1998

Journal of Biological Chemistry

118

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We have recently discovered an alternative function of the putative metastasis suppressor protein Nm23, which is identical to nucleoside diphosphate kinase, as a protein phosphotransferase in vitro. While purified native Nm23 protein did not phosphorylate other proteins, we could purify a Nm23-associated protein that activates the protein phosphotransferase function; it was identified as a glyceraldehyde-3-phosphate dehydrogenase (GAPDH) isoenzyme. Co-expression and purification of (His) 6 -tagged GAPDH in combination with either Nm23-H1 or Nm23-H2 in baculovirus-infected Sf9 cells showed that only Nm23-H1, but not Nm23-H2, forms a stable complex with GAPDH. Protein phosphotransferase activity was confirmed for the recombinant GAPDH⅐Nm23-H1 complex but not for either of the enzymes alone, nor was this activity observed after simple mixing of the purified proteins in vitro. The molecular mass of the highly purified recombinant GAPDH⅐ Nm23-H1 complex suggests that a dimer of GAPDH interacts with a dimer of Nm23-H1. In contrast to the complex with GAPDH, co-expression of Nm23-H1 with antioxidant protein (MER-5) or creatine kinase did not activate the protein phosphotransferase function, indicating that this activation may specifically require GAPDH as a binding partner.The first member of the nm23 gene family has been isolated due to its reduced expression in highly metastatic clones of murine melanoma cells as compared with their nonmetastatic counterparts (1). The proposed metastasis suppressor activity of this gene, now termed nm23-H1, has subsequently been confirmed in numerous functional studies: transfection of nm23-H1 cDNA into highly metastatic melanoma or mamma carcinoma cell lines resulted in a significant reduction of metastatic potential in vivo (2-5). In many human tumors, such as mammary carcinomas, hepatocellular carcinomas, and malignant melanomas, reduced expression of nm23 was correlated with lymph node metastasis and decreased disease-free survival of the patients (reviewed in Ref. 6). In other tumor types, however, increased expression of nm23 was associated with cell proliferation and advanced stages of the disease (7, 8), suggesting complex biological functions of the gene product(s). The later cloned gene nm23-H2, although 81% identical to nm23-H1, provided little or no evidence for a metastasis suppressor activity in tumor expression studies and in a transfection assay (3, 9 -12). Two further members of the nm23 gene family, DR-nm23 (13) and nm23-H4 (14), are more distantly related to the first discovered genes and no experimental data are known so far regarding their metastasis suppressor potential. The biochemical mechanism(s) underlying the antimetastatic properties of Nm23-H1 are unknown. All nm23 genes as known today have been demonstrated to encode for nucleoside diphosphate (NDP) 1 kinases. These long known enzymes are ubiquitously expressed and remarkably conserved throughout evolution. For example, the human NDP kinase is 80, 62, and 40% identical to the NDP kinases from Drosophila,...

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“…Subsite 2, interacting with ICAM-1 C-terminal residues (present in C27-Cl5 ICAM-1 peptides), may either overhp with the enzyme catalytic site or be indirectly involved in the activity-associated conformational changes of the active site, induced by NAD' . Interestingly, the existence of two classes of binding sites for tubulin on GraP-DH, of high and low affinity respectively, has been suggested, only the binding to high-affinity sites being correlated with inhibition of GraP-DH glycolytic activity [32].…”

Section: Discussionmentioning

confidence: 99%

Association of the Cytoplasmic Domain of Intercellular‐Adhesion Molecule‐1 with Glyceraldehyde‐3‐Phosphate Dehydrogenase and β‐Tubulin

Federici

Camoin

Hattab

et al. 1996

European Journal of Biochemistry

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To elucidate the molecular mechanisms of the transendothelial migration of leukocytes, we attempted to identify the cellular proteins capable of interaction with the cytoplasmic domain of the intercellular adhesion molecule-I (ICAM-1) in a rat brain microvessel endothelial cell line (RBE4 cells). A 27-aminoacid synthetic peptide, corresponding to the cytoplasmic domain of rat ICAM-1, was covalently linked to a Sepharose matrix. Upon affinity chromatography of RBE4 cell cytosol, several ICAM-1-interacting proteins were specifically eluted by the soluble peptide. Two of these proteins have been identified by microsequencing as the cytoskeletal protein P-tubulin and the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GraP-DH). Experiments carried out with purified GraP-DH or CNBr fragments of GraP-DH indicated that binding to the ICAM-1 matrix was mediated by the C-terminal domain of GraP-DH, containing the binding site of the cofactor NAD+, and that NAD' could compete with this binding. Using a series of ICAM-1 C-terminal truncated peptides, we could demonstrate that (a) the nitric-oxideinduced covalent linkage of NAD' to GraP-DH was impaired by these peptides, (b) the glycolytic activity of GraP-DH was drastically inhibited by a truncated peptide containing the 15 C-terminal residues, (c) nitric oxide appeared to prevent this inhibition.Together, our results demonstrate that GraP-DH specifically associate! with the isolated ICAM-1 cytoplasmic domain. Since GraP-DH is known as a microtubule bundling protein, these findings suggest that, in a cellular environment, GraP-DH may behave as an adaptor molecule by linking ICAM-1 to the microtubule network. The role of nitric oxide in the modulation of this interaction deserves further investigation.

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Binding Constants and Stoichiometries of Glyceraldehyde 3-Phosphate Dehydrogenase-Tubulin Complexes

Cited by 61 publications

References 0 publications

A Dimer Interface Mutation in Glyceraldehyde-3-Phosphate Dehydrogenase Regulates Its Binding to AU-rich RNA

A Dimer Interface Mutation in Glyceraldehyde-3-Phosphate Dehydrogenase Regulates Its Binding to AU-rich RNA

Glyceraldehyde-3-phosphate Dehydrogenase and Nm23-H1/Nucleoside Diphosphate Kinase A

Association of the Cytoplasmic Domain of Intercellular‐Adhesion Molecule‐1 with Glyceraldehyde‐3‐Phosphate Dehydrogenase and β‐Tubulin

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