Adiponectin Lowers Glucose Production by Increasing SOGA

B., Cowerd, Rachael; Asmar, Melissa M.; Alderman, J. Mc Kee; A., Alderman, Elizabeth; Garland, Alaina L.; Busby, Walker H.; Bodnar, Wanda M.; Rusyn, Ivan; Medoff, Benjamin D.; Tisch, Roland; Mayer‐Davis, Elizabeth J.; Swenberg, James A.; Zeisel, Steven H.; Combs, Terry P.

doi:10.2353/ajpath.2010.100363

Cited by 35 publications

(37 citation statements)

References 51 publications

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“…interactome, SOGA1 is a relatively uncharacterized protein that has been linked to the regulation of autophagy in hepatocytes (82). In response to nutritional deprivation, autophagy can initiate the release of glucose from the liver by promoting the hydrolysis of proteins, glycogen, and triglycerides (100-102).…”

Section: Discussionmentioning

confidence: 99%

Characterization of the CLASP2 Protein Interaction Network Identifies SOGA1 as a Microtubule-Associated Protein

Kruse

Krantz

Barker

et al. 2017

Molecular & Cellular Proteomics

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SummaryCLASP2 is a microtubule-associated protein that undergoes insulin-stimulated phosphorylation and co-localization with reorganized actin and GLUT4 at the plasma membrane.To gain insight to the role of CLASP2 in this system, we developed and successfully executed a streamlined interactome approach and built a CLASP2 protein network in 3T3-L1 adipocytes.Using two different commercially available antibodies for CLASP2 and an antibody for epitopetagged, overexpressed CLASP2, we performed multiple affinity purification coupled with mass spectrometry (AP-MS) experiments in combination with label-free quantitative proteomics and analyzed the data with the bioinformatics tool Significance Analysis of Interactome (SAINT). We discovered that CLASP2 co-immunoprecipitates (co-IPs) the novel protein SOGA1, the microtubule-associated protein kinase MARK2, and the microtubule/actin-regulating protein G2L1. The GTPase-activating proteins AGAP1 and AGAP3 were also enriched in the CLASP2 interactome, although subsequent AGAP3 and CLIP2 interactome analysis suggests a preference of AGAP3 for CLIP2. Follow-up MARK2 interactome analysis confirmed reciprocal co-IP of CLASP2 and also revealed MARK2 can co-IP SOGA1, glycogen synthase, and glycogenin.Investigating the SOGA1 interactome confirmed SOGA1 can reciprocal co-IP both CLASP2 and MARK2 as well as glycogen synthase and glycogenin. SOGA1 was confirmed to colocalize with CLASP2 and also with tubulin, which identifies SOGA1 as a new microtubule-associated protein.These results introduce the metabolic function of these proposed novel protein networks and their relationship with microtubules as new fields of cytoskeleton-associated protein biology. 5

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Section: Discussionmentioning

confidence: 99%

Characterization of the CLASP2 Protein Interaction Network Identifies SOGA1 as a Microtubule-Associated Protein

Kruse

Krantz

Barker

et al. 2017

Molecular & Cellular Proteomics

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“…Recently, public databases have been adopting the name 'SOGA2' for MTCL1, which is probably because a recent paper that named its paralog molecule suppressor of glucose by autophagy (SOGA) (Cowerd et al, 2010). The paper argued that the 'MTCL1 paralog' was secreted as 80 kDa and 25 kDa peptides after excision of an 'internal peptide sequence' and mediated adiponectin-dependent suppression of glucose production by inhibiting autophagy.…”

Section: Discussionmentioning

confidence: 99%

A novel PAR-1-binding protein, MTCL1, plays critical roles in organizing microtubules in polarizing epithelial cells

Sato

Akitsu

Amano

et al. 2013

Journal of Cell Science

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SummaryThe establishment of epithelial polarity is tightly linked to the dramatic reorganization of microtubules (MTs) from a radial array to a vertical alignment of non-centrosomal MT bundles along the lateral membrane, and a meshwork under the apical and basal membranes. However, little is known about the underlying molecular mechanism of this polarity-dependent MT remodeling. The evolutionarily conserved cell polarity-regulating kinase PAR-1 (known as MARK in mammals), whose activity is essential for maintaining the dynamic state of MTs, has indispensable roles in promoting this process. Here, we identify a novel PAR-1-binding protein, which we call microtubule crosslinking factor 1 (MTCL1), that crosslinks MTs through its N-terminal MT-binding region and subsequent coiledcoil motifs. MTCL1 colocalized with the apicobasal MT bundles in epithelial cells, and its knockdown impaired the development of these MT bundles and the epithelial-cell-specific columnar shape. Rescue experiments revealed that the N-terminal MT-binding region was indispensable for restoring these defects of the knockdown cells. MT regrowth assays indicated that MTCL1 was not required for the initial radial growth of MTs from the apical centrosome but was essential for the accumulation of non-centrosomal MTs to the sublateral regions. Interestingly, MTCL1 recruited a subpopulation of PAR-1b (known as MARK2 in mammals) to the apicobasal MT bundles, and its interaction with PAR-1b was required for MTCL1-dependent development of the apicobasal MT bundles. These results suggest that MTCL1 mediates the epithelial-cell-specific reorganization of non-centrosomal MTs through its MT-crosslinking activity, and cooperates with PAR-1b to maintain the correct temporal balance between dynamic and stable MTs within the apicobasal MT bundles.

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“…The search for an inhibitor of autophagy in the adiponectin signaling pathway led to the discovery of a previously unknown protein called the Suppressor of Glucose from Autophagy ( SOGA ) (Figure 5) [89]. Proteomic analysis shows that HMW and LMW adiponectin upregulate SOGA in hepatoma and hepatocyte cultures.…”

Section: Suppression Of Gluconeogenic Substrate Availabilitymentioning

confidence: 99%

Adiponectin signaling in the liver

Combs

Marliss

2013

Rev Endocr Metab Disord

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134

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High glucose production contributes to fed and fasted hyperglycemia in Type 1 Diabetes (T1D) and Type 2 Diabetes (T2D). The breakdown of the adiponectin signaling pathway in T1D and the reduction of circulating adiponectin in T2D contribute to this abnormal increase in glucose production. Sufficient amounts of insulin could compensate for the loss of adiponectin signaling in T1D and T2D and reduce hyperglycemia. However, the combination of low adiponectin signaling and high insulin resembles an insulin resistance state associated with cardiovascular disease and decreased life expectancy. Future development of medications that correct the deficiency of adiponectin signaling in the liver could restore the metabolic balance in T1D and T2D and reduce the need for insulin. This article reviews the adiponectin signaling pathway in the liver through T-cadherin, AdipoR1, AdipoR2, AMPK, ceramidase activity, APPL1 and the recently discovered Suppressor Of Glucose from Autophagy (SOGA).

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Adiponectin Lowers Glucose Production by Increasing SOGA

Cited by 35 publications

References 51 publications

Characterization of the CLASP2 Protein Interaction Network Identifies SOGA1 as a Microtubule-Associated Protein

Characterization of the CLASP2 Protein Interaction Network Identifies SOGA1 as a Microtubule-Associated Protein

A novel PAR-1-binding protein, MTCL1, plays critical roles in organizing microtubules in polarizing epithelial cells

Adiponectin signaling in the liver

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