Glyceraldehyde-3-phosphate Dehydrogenase Is Phosphorylated by Protein Kinase Cι/λ and Plays a Role in Microtubule Dynamics in the Early Secretory Pathway

Tisdale, Ellen J.

doi:10.1074/jbc.m109744200

Cited by 151 publications

(137 citation statements)

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“…More recently, GAPDH has been found to associate with ␤-tubulin recruitment to membrane (26,28). Thus, an association appears to exist between GAPDH and microtubule remodeling.…”

Section: Discussionmentioning

confidence: 99%

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Identification ofMycobacterium aviumpathogenicity island important for macrophage and amoeba infection

Danelishvili

Stang

et al. 2007

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

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The ability to infect macrophages is a common characteristic shared among many mycobacterial species. Mycobacterium avium, Mycobacterium tuberculosis, and Mycobacterium kansasii enter macrophages, using the complement receptors CR1, CR3, CR4, and the mannose receptor. To identify M. avium genes and host cell pathways involved in the bacterial uptake by macrophages, we screened a M. avium transposon mutant library for the inability to enter macrophages. Uptake-impaired clones were selected. Sequence of six M. avium clones identified one gene involved in glycopeptidolipid biosynthesis, one gene encoding the conserved membrane protein homologue to the M. avium subsp. paratuberculosis MAP2446c gene and four others belonging to the same region of the chromosome. Analysis of the chromosome region revealed a pathogenicity island inserted between two tRNA sequences with 58% of G؉C content versus 69% in the M. avium genome. The region is unique for M. avium and is not present in M. tuberculosis or M. paratuberculosis. Although the mutants did not differ from the WT bacterium regarding the binding to macrophage cell membrane, analysis of macrophage proteins after 1 h infection revealed a deficiency in the mutant to phosphorylate certain proteins on uptake. To understand M. avium interaction with two evolutionarily distinct hosts, the mutants were evaluated for Acanthamoeba castellanii invasion. The defect in the ability of the mutants to invade both cells was highly similar, suggesting that M. avium might have evolved mechanisms that are used to enter amoebas and human macrophages. uptake M ycobacterium avium complex is an intracellular pathogen that can infect a variety of host cells (1-4). M. avium, like the majority of pathogenic mycobacteria, infects and replicates within macrophages (5, 6), which are the phagocytic cells where M. avium establishes a long-term infection (7).A number of studies in vitro have determined that M. avium, in a manner similar to Mycobacterium tuberculosis, is taken up by macrophages using the complement receptors CR3, CR4, and CR1 (8-10), and/or the mannose receptor (8, 11). M. tuberculosis has been found to bind to the CD11b chain of the ␤-integrin of the CR3 and CR4 receptors, which happened without participation of the serum complement proteins (10). Other studies demonstrated that the mannose capped lipoarabinomannan antigen of virulent M. tuberculosis cell wall is capable to recognize and bind to the mannose receptors on the macrophage membrane (11).It has been hypothesized that virulent mycobacteria bind to many receptors because pathogenic mycobacteria would use several different receptors on the macrophage membrane to be internalized, as a strategy to guarantee phagocytosis, even when a sitespecific macrophage would not contain one or more membrane receptors. In addition, this property would address the possibility that mycobacteria may not express all of the ligands during all phases of infection. Most mycobacteria evolved to survive inside phagocytic cells, although they can enter ...

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“…More recently, GAPDH has been found to associate with ␤-tubulin recruitment to membrane (26,28). Thus, an association appears to exist between GAPDH and microtubule remodeling.…”

Section: Discussionmentioning

confidence: 99%

“…Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been described on the surface of phagocytic cells and has a role in signal transduction (26)(27)(28). More recently, GAPDH has been found to associate with ␤-tubulin recruitment to membrane (26,28).…”

Section: Discussionmentioning

confidence: 99%

Identification ofMycobacterium aviumpathogenicity island important for macrophage and amoeba infection

Danelishvili

Stang

et al. 2007

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

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“…Both Src and GAPDH bind to the aPKC/ regulatory domain (13,20). The interaction between GAPDH and aPKC/ can be partly blocked in the presence of a peptide made to the unique aPKC/ pseudosubstrate region (13).…”

Section: Discussionmentioning

confidence: 99%

“…His 6 -GST Pull-down-The transient expression of His 6 -PKC/ was performed as described (4,13). The supernatant that contained overexpressed His 6 -tagged PKC/ was applied to a 2-ml column of Ni 2ϩ -NTA-agarose (Qiagen, Valencia, CA) equilibrated in buffer A (10 mM Hepes, pH 7.9, 5 mM MgCl 2 , 0.1 mM EDTA, 50 mM NaCl, and 0.8 mM imidazole).…”

Section: Methodsmentioning

confidence: 99%

“…The Rab2-generated vesicles are devoid of secretory cargo but contain aPKC/, ␤-coat protein (␤-COP), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and the recycling protein p53/p58, suggesting that these carriers traffic in the retrograde pathway (11,12). GAPDH also interacts directly with Rab2 as well as aPKC/ and additionally serves as a substrate for the kinase (13,14). Although GAPDH is essential for membrane trafficking in the early secretory pathway independent of catalytic activity, the precise role of this glycolytic enzyme in transport is unclear (14).…”

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confidence: 99%

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Src-dependent aProtein Kinase C ι/λ (aPKCι/λ) Tyrosine Phosphorylation Is Required for aPKCι/λ Association with Rab2 and Glyceraldehyde-3-phosphate Dehydrogenase on Pre-Golgi Intermediates

Tisdale

Artalejo

2006

Journal of Biological Chemistry

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The small GTPase Rab2 is required for membrane transport between the endoplasmic reticulum (ER) and the Golgi complex. Rab2 associates with pre-Golgi intermediates (also termed vesicular tubular clusters; VTCs) that sort cargo to the anterograde pathway from recycling proteins retrieved to the ER. Our previous studies have shown that Rab2 stimulates atypical protein kinase C / (aPKC/) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) recruitment to VTCs. Both aPKC/ and GAPDH bind directly to Rab2 and aPKC/ and GAPDH interact. Based on the reports demonstrating aPKC-Src interaction and Src activity in the retrograde pathway (Golgi-ER), studies were initiated to learn whether Rab2 also promoted Src recruitment to VTCs. Using a quantitative membrane binding assay, we found that Rab2-stimulated Src membrane association in a dose-dependent manner. The recruited Src binds to aPKC/ and GAPDH on the membrane; however, Src does not interact with Rab2. The membrane-associated Src tyrosine phosphorylates aPKC/ on the VTC. To determine the consequence of aPKC/ tyrosine phosphorylation, the membrane binding assay was supplemented with the Src-specific tyrosine kinase inhibitor 4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo(3,4-d)pyrimidine (PP2). Although Rab2, Src, and GAPDH recruitment was not affected, the Rab2-PP2-treated membranes contained a negligible amount of aPKC/. Since Rab2 requires aPKC/ for the downstream recruitment of ␤-coat protein (␤-COP) to VTCs, the Rab2-PP2-treated membranes were evaluated for the presence of ␤-COP. Like aPKC/, the membranes contained a negligible amount of ␤-COP that was reflected by the drastic reduction in Rab2-dependent vesicle formation. These data suggest that Src-mediated tyrosine phosphorylation of aPKC/ facilitates aPKC/ association with Rab2-Src-GAPDH on VTCs, which is ultimately necessary for the downstream recruitment of ␤-COP and release of Rab2-mediated retrograde-directed vesicles.

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Biological Consequences of Protein Moonlighting

2016

Protein Moonlighting in Biology and Medicine

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Glyceraldehyde-3-phosphate Dehydrogenase Is Phosphorylated by Protein Kinase Cι/λ and Plays a Role in Microtubule Dynamics in the Early Secretory Pathway

Cited by 151 publications

References 53 publications

Identification ofMycobacterium aviumpathogenicity island important for macrophage and amoeba infection

Identification ofMycobacterium aviumpathogenicity island important for macrophage and amoeba infection

Src-dependent aProtein Kinase C ι/λ (aPKCι/λ) Tyrosine Phosphorylation Is Required for aPKCι/λ Association with Rab2 and Glyceraldehyde-3-phosphate Dehydrogenase on Pre-Golgi Intermediates

Biological Consequences of Protein Moonlighting

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