Starch binding domain-containing protein 1/genethonin 1 is a novel participant in glycogen metabolism.

Abstract

Since publication of this article, we have become aware of an error in the experimental protocol to visualize LAMP1 in cells by immunofluorescence. Specifically, the wrong antibodies were used, so assessments of LAMP1 distribution are not reliable. We did additional experiments, including analysis of the distribution of LAMP2, which is found in the same compartments as LAMP1. We observed no co-localization of LAMP2 and Stbd1. However, the primary conclusion of the study, the link between Stbd1 and glycogen metabolism, is unaffected, as is our hypothesis that Stbd1 anchors glycogen to membranes and may be involved in its localization and trafficking within the cell. The grant information footnote should read as follows. This work was supported, in whole or in part, by National Institutes of Health Grants R01 CA42755 and CA85804 (to C. W. D.), R01 AG031903 (to S. M.), T32 HL007147 (to S. S. and J. K. M.), and T32 GM007250 (to J. K. M.). The "Acknowledgments" should read as follows. The Dig2/RTP801 knock-out mice were obtained from Quark Pharmaceuticals, Inc., for whom they were exclusively generated at Lexicon. We thank Tamotsu Yoshimori and Noboru Mizushima for providing LC3 cDNA and Mark Jackson for suggestions regarding lentiviral shRNA. This work was supported in part by an Ohio Center for Innovative Immunosuppressive Therapeutics grant, which maintains the spinning disk confocal microscope in the Morphology Core Facility of the Department of Dermatology, Case Western Reserve University.THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 286, NO. 45, p. 39673, November 11, 2011 © 2011 ADDITIONS AND CORRECTIONS This paper is available online at www.jbc.orgWe suggest that subscribers photocopy these corrections and insert the photocopies in the original publication at the location of the original article. Authors are urged to introduce these corrections into any reprints they distribute. Secondary (abstract) services are urged to carry notice of these corrections as prominently as they carried the original abstracts.

Stbd1 is highly elevated in skeletal muscle of Pompe disease mice but suppression of its expression does not affect lysosomal glycogen accumulation

“…Primary antibodies used: rabbit anti mouse Stbd1, gift from Dr. Peter J. Roach, Indiana University [8]; LAMP2 and rabbit anti PYGM (Abcam); rabbit anti glycogen synthase (Cell Signaling); goat anti GAPDH (Novus Biologicals); rabbit anti LC3B; and HRP-conjugated mouse anti β-actin (Sigma-Aldrich).…”

“…Starch binding domain containing protein 1 (Stbd1, also known as GENX-3414 or genethonin 1) is a protein with a predicated structure containing a hydrophobic N terminus and a C-terminal CBM20 glycan binding domain [6,7]. Stbd1 is highly expressed in muscle and liver, the major tissues of glycogen storage [6,8]. The function of Stbd1 was unknown but recent studies demonstrated that it is involved in glycogen metabolism [8,9].…”

“…Stbd1 is highly expressed in muscle and liver, the major tissues of glycogen storage [6,8]. The function of Stbd1 was unknown but recent studies demonstrated that it is involved in glycogen metabolism [8,9]. In mice, genetic deletion of muscle glycogen synthase caused a complete loss of Stbd1 protein expression in muscle while liver glycogen synthase knockout led to a 40% reduction of Stbd1 [8].…”

“…The function of Stbd1 was unknown but recent studies demonstrated that it is involved in glycogen metabolism [8,9]. In mice, genetic deletion of muscle glycogen synthase caused a complete loss of Stbd1 protein expression in muscle while liver glycogen synthase knockout led to a 40% reduction of Stbd1 [8]. In cultured cells, Stbd1 locates to perinuclear compartments and co-localized with glycogen, the lysosomal marker LAMP1 but not the autophagic marker LC3 [8].…”

“…In mice, genetic deletion of muscle glycogen synthase caused a complete loss of Stbd1 protein expression in muscle while liver glycogen synthase knockout led to a 40% reduction of Stbd1 [8]. In cultured cells, Stbd1 locates to perinuclear compartments and co-localized with glycogen, the lysosomal marker LAMP1 but not the autophagic marker LC3 [8]. These results strongly suggest that Stbd1 is a specific mediator for cytoplasmic glycogen transport into the lysosome and could potentially be a new therapeutic target for Pompe disease.…”