Starch Binding Domain-containing Protein 1 Plays a Dominant Role in Glycogen Transport to Lysosomes in Liver

Sun, Tao; Yi, Haiqing; Yang, Chunyu; Kishnani, Priya S.; Sun, Baodong

doi:10.1074/jbc.c116.741397

Cited by 42 publications

(43 citation statements)

References 27 publications

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“…(29) In this respect, a recent study indeed indicates that lysosomal glycogen breakdown and autophagosome formation are differentially regulated. (30) Our data appear contradictory to findings reported by Rother and Schwenk, who concluded that increased glycogen cycling cannot account for residual EGP in GSD I. Using enteral infusion of 13 C-glucose and galactose, these investigators found that increased glucose infusion suppressed EGP in GSD I patients but simultaneously enhanced UDP-glucose turnover.…”

Section: Discussioncontrasting

confidence: 99%

Hepatocytes contribute to residual glucose production in a mouse model for glycogen storage disease type Ia

et al. 2017

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Our data indicate that hepatocytes contribute to residual glucose production in GSD Ia. We show that α-glucosidase activity, i.e. glycogen debranching and/or lysosomal glycogen breakdown, contributes to residual glucose production by GSD Ia hepatocytes. A strong reduction in hepatic GCK flux in L-G6pc-/- mice furthermore limits the phosphorylation of free glucose synthesized by G6pc-deficient hepatocytes, allowing the release of glucose into the circulation. The almost complete abrogation of GCK flux in G6pc-deficient liver also explains the contradictory reports on residual glucose production in GSD Ia patients. (Hepatology 2017;66:2042-2054).

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Section: Discussioncontrasting

confidence: 99%

Hepatocytes contribute to residual glucose production in a mouse model for glycogen storage disease type Ia

et al. 2017

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“…STBD1 is a N-terminally membrane anchored [38] glycogen-binding [25,39] protein that localizes glycogen to perinuclear sites/ER, late endosomes and lysosomes and is most abundantly expressed in muscle and liver [25]. The lower expression of STBD1 we observed in CCF together with its involvement in the lysosomal glycogen degradation pathway [27] suggests that this reduction of STBD1expression could be an additional factor contributing to glycogen accumulation in CCF. However, a significant glycogen accumulation in livers of Stbd1-KO mice was not observed.…”

Section: Stbd1mentioning

confidence: 68%

“…An Atg8 family interacting motif (AIM) and interaction with GABARAPL1 implicated STBD1 to be involved in autophagic glycogen degradation, so called glycophagy [26]. In a mouse model of Pompe disease, deletion of STBD1 suppressed lysosomal glycogen accumulation, suggesting STDB1 to be involved in transfer of glycogen from the cytoplasm to lysosomes [27]. The reduced expression of STBD1 in CCF could be responsible for the hepatocellular glycogen accumulation.…”

Section: Loss Of Stbd1 In Mice Does Not Cause Glycogen Accumulation Imentioning

confidence: 99%

“…This was unexpected, as 10% of glycogen degraded in the liver passes through the lysosomal pathway [40] and the loss of STBD1 should result in an appreciable accumulation of glycogen in the liver. One explanation for the lack of this glycogen accumulation is the compensation of STBD1-mediated glycogen translocation into lysosomes by cytoplasmic glycogen degradation Alternative mechanisms of glycogentranslocation are also possible, as the loss of STBD1 in a mouse model of lysosomal glycogen overload (acid alpha-glucosidase-KO mice) did not completely antagonized lysosomal glycogen accumulation [27]. Hence, we conclude that reduction of STBD1 in CCF may only contribute to glycogen accumulation in combination with yet unidentified factors that favor lysosomal glycogen degradation.…”

Section: Stbd1mentioning

confidence: 99%

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Transcriptomic and Proteomic analysis of clear cell foci (CCF) in the human non-cirrhotic liver identifies several differentially expressed genes and proteins with functions in cancer cell biology and glycogen metabolism

Metzendorf

Wineberger

Rausch

et al. 2020

Preprint

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Clear cell foci (CCF) of the liver are considered to be pre-neoplastic lesions of hepatocellular adenomas and carcinomas. They are hallmarked by glycogen-overload and activation of AKT/mTOR-signaling. Here we report the transcriptome and proteome of CCF extracted from human liver biopsies by laser capture microdissection. We mainly found genes and proteins with lower expression in CCF compared to control samples. Of 14 differentially expressed transcripts only 3 were overexpressed and belong to previously uncharacterized long non-coding RNAs. At the protein level, 3 proteins were at least 1.5-fold higher expressed in CCF than in control samples, while 22 proteins were at least 1.5-fold less abundant. Using immunohistochemistry, the reduced expressions of STBD1, USP28, monad/WDR92, CYB5B and HSPE1 were validated in CCF. Knockout of STBD1, the gene coding for Starch-binding domain-containing protein 1, in mice did not have an effect on liver glycogen levels. Similiarly, Usp28 knockout in mice did not affect glycogen storage in diethylnitrosamine-induced liver carcinoma. Thus, these data indicate that reduced expression of STBD1 or USP28 in CCF is unlikely to explain glycogen overload. Our study revealed several novel proteins and RNAs that are differentially expressed in CCF and have functions relevant for carcinogenesis or the glycogen metabolism.

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“…SBDs were originally recognized as a module found typically in microbial amylolytic and related enzymes. It is worth mentioning that various SBDs and GBDs have also been identified in other plant and animal enzymes and proteins, such as plant starch synthase III, glucan‐water dikinases, starch‐excess protein‐4, animal laforin, genethonin‐1, as well as the β‐subunit of AMP‐activated protein kinase and its homologues in plants, and even in lytic polysaccharide monooxygenases from fungi . Nevertheless, as for the microbial SBDs, generally the non‐microbial SBDs or GBDs are always involved in metabolism of starch and/or glycogen, or other α‐glucans …”

Section: Introductionmentioning

confidence: 99%

The starch‐binding domain family CBM41—An in silico analysis of evolutionary relationships

et al. 2017

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Within the CAZy database, there are 81 carbohydrate‐binding module (CBM) families. A CBM represents a non‐catalytic domain in a modular arrangement of glycoside hydrolases (GHs). The present in silico study has been focused on starch‐binding domains from the family CBM41 that are usually part of pullulanases from the α‐amylase family GH13. Currently there are more than 1,600 sequences classified in the family CBM41, almost exclusively from Bacteria, and so a study was undertaken in an effort to divide the members into relevant groups (subfamilies) and also to contribute to the evolutionary picture of family CBM41. The CBM41 members adopt a β‐sandwich fold (∼100 residues) with one carbohydrate‐binding site formed by the side‐chains of three aromatic residues that interact with carbohydrate. The family CBM41 can be divided into two basic subdivisions, distinguished from each other by a characteristic sequence pattern or motif of the three essential aromatics as follows: (i) “W‐W‐∼10aa‐W” (the so‐called Streptococcus/Klebsiella‐type); and (ii) “W‐W‐∼30aa‐W” (Thermotoga‐type). Based on our bioinformatics analysis it is clear that the first and second positions of the motif can be occupied by aromatic residues (Phe, Tyr, His) other than tryptophan, resulting in the existence of six different carbohydrate‐binding CBM41 groups, that reflect mostly differences in taxonomy, but which should retain the ability to bind an α‐glucan. In addition, three more groups have been proposed that, although lacking the crucial aromatic motif, could possibly employ other residues from remaining parts of their sequence for binding carbohydrate. Proteins 2017; 85:1480–1492. © 2017 Wiley Periodicals, Inc.

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Starch Binding Domain-containing Protein 1 Plays a Dominant Role in Glycogen Transport to Lysosomes in Liver

Cited by 42 publications

References 27 publications

Hepatocytes contribute to residual glucose production in a mouse model for glycogen storage disease type Ia

Hepatocytes contribute to residual glucose production in a mouse model for glycogen storage disease type Ia

Transcriptomic and Proteomic analysis of clear cell foci (CCF) in the human non-cirrhotic liver identifies several differentially expressed genes and proteins with functions in cancer cell biology and glycogen metabolism

The starch‐binding domain family CBM41—An in silico analysis of evolutionary relationships

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