GABARAPL2 Antibody
- Known as:
- GABARAPL2 Antibody
- Catalog number:
- XW-7929
- Product Quantity:
- 0.05 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- GABARAPL2 Antibody
Related genes to: GABARAPL2 Antibody
- Gene:
- GABARAPL2 NIH gene
- Name:
- GABA type A receptor associated protein like 2
- Previous symbol:
- -
- Synonyms:
- GEF2, ATG8, GATE16, GATE-16, ATG8C
- Chromosome:
- 16q23.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-07-09
- Date modifiied:
- 2016-10-05
Related products to: GABARAPL2 Antibody
Related articles to: GABARAPL2 Antibody
- - Source: PubMed
Publication date: 2026/01/21
Yu Shu-FanKimaro John PraygodZhou XuLi ShuangZheng Li-BingChi Chang-Feng - Glycophagy, a selective form of autophagy critical for glycogen homeostasis, relies on the glycogen cargo receptor called starch-binding domain-containing protein 1 (STBD1), yet its evolutionary origins remain elusive. Here, we provide evidence that the Pacific oyster Crassostrea gigas utilizes glycophagy to manage glycogen mobilization during periods of energy deprivation. We identify an oyster STBD1 protein, and trace its origins through phylogenetic and comparative genomic analysis of the carbohydrate binding module family 20 (CBM20) domain within this protein across metazoans. Oyster STBD1 and those in other invertebrates contain an N-terminal CBM20, contrasting the C-terminal location of CBM20 in vertebrate STBD1. N-terminal CBM20 STBD1 proteins have a deep origin in bilaterians, with the vertebrate structural arrangement arising at the chordate root. Structural modelling and functional studies reveal that the N-terminal organization of the CBM20 domain in STBD1 enhances glycogen binding, with subsequent anchoring by GABARAPL2, facilitating an increased glycogen flux into autophagosomes for lysosomal degradation. We conclude that glycophagy is deeply conserved in bilaterians and that STBD1 structural evolution underlies potentially adaptive variation in metabolic strategies across distinct animal clades. - Source: PubMed
Publication date: 2026/01/20
Ren LitingBai YitianShi ChenyuHao ZhengwangLi QiMacqueen Daniel JLiu Shikai - Preterm infants are at risk for bilirubin-induced brain injury. Phototherapy is effective for lowering serum bilirubin but has potential adverse effects. The independent effects of hyperbilirubinemia and phototherapy on the hippocampal gene expression profile were determined using a preterm-equivalent Gunn rat model. - Source: PubMed
Publication date: 2025/12/22
Satrom Katherine MLock Eric FLund Troy CTran Phu VRao Raghavendra B - Although we now have a rich toolset for genome editing, an equivalent framework for manipulating the proteome with a comparable flexibility and specificity remains elusive. A promising strategy for "proteome editing" is to use bifunctional molecules ( PROteolysis-Targeting Chimeras or PROTACs) that bring a target protein into proximity with a degradation or stabilization effector, but their broader application is constrained by a limited repertoire of well-characterized target or effector "handles". We asked whether coupling protein design to a multiplex screening framework could address this gap by accelerating the discovery of effector handles for intracellular protein degradation, stabilization, or relocalization. Using LABEL-seq, a sequencing-based assay that enables multiplex, quantitative measurement of protein abundance, we screened 9,715 designed candidate effector handles for their ability to recruit a target protein to components of the ubiquitin-proteasome system (UPS) (FBXL12, TRAF2, UCHL1, USP38) or the autophagy pathway (GABARAP, GABARAPL2, MAP1LC3A). In a single experiment, we discovered hundreds of designed effector handles that reproducibly drove either intracellular degradation (n = 277) or stabilization (n = 204) of a reporter protein. Validation of a subset of these hits in an orthogonal assay confirmed that sequencing-based measurements from the primary screen reliably reflected changes in intracellular abundance of the target protein. Successful effector handles were discovered for both the UPS (n = 194) and autophagy (n = 287) pathways, which provide complementary routes for programmable proteome editing. Autophagy-recruiting effector handles generalized to endogenous targets, as substituting the reporter-specific target handle with a high-affinity MCL1 binder reduced endogenous levels of this intracellular oncoprotein. Moreover, directing autophagy-recruiting effector handles to the outer mitochondrial membrane dramatically perturbed mitochondrial networks in a manner consistent with synthetic tethering and sequestration. Beyond generating a diverse repertoire of protein abundance or localization effector handles, our results establish a scalable, low-cost platform that links deep learning-guided protein design to functional cellular readouts, and chart a course toward a general framework for programmable proteome editing. - Source: PubMed
Publication date: 2025/10/13
Suiter Chase CAhn GreenChiu MelodieFu YiSadre ShayanSimon Jessica JLee David SFowler Douglas MMaly Dustin JBaker DavidShendure Jay - Loss-of-function variants in TBK1, encoding a protein kinase, are strongly associated with familial amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). However, how haploinsufficiency for TBK1 leads to age-related neurodegeneration remains unresolved. Here, we utilize sets of isogenic induced pluripotent stem cells (iPSCs) with loss of TBK1 or loss of optineurin (OPTN) for quantitative global proteomics and phospho-proteomics in both stem cells and excitatory neurons. We found that TBK1 sustains the abundance and phosphorylation of its interacting adapter proteins, AZI2/NAP1, TANK, and TBKBP1/SINTBAD. Moreover, TBK1 regulates the phosphorylation of endo-lysosomal proteins, such as GABARAPL2, the late-endosome GTPase RAB7A, and selective autophagy cargo receptor proteins-including novel phospho-sites in p62/SQSTM1-in neurons. Finally, we provide a census of the phospho-proteome in nascent human neurons for further studies. Overall, TBK1 serves as a point of convergence in ALS/FTD-linked endo-lysosomal networks that act in a cell-autonomous manner to maintain protein homeostasis in neurons. - Source: PubMed
Publication date: 2025/10/29
Smeyers JulieOses-Prieto Juan AYadanar LinWang ManIadarola MarciLu SerenaWang Karen SWatanabe Taylor HDebnath JayantaBurlingame Alma LMordes Daniel A