GORASP2

Last update 08 May 2025

Basic Info

Synonyms

Golgi phosphoprotein 6, golgi reassembly stacking protein 2, Golgi reassembly-stacking protein 2

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Introduction

Key structural protein of the Golgi apparatus (PubMed:33301566). The membrane cisternae of the Golgi apparatus adhere to each other to form stacks, which are aligned side by side to form the Golgi ribbon (PubMed:33301566). Acting in concert with GORASP1/GRASP65, is required for the formation and maintenance of the Golgi ribbon, and may be dispensable for the formation of stacks (PubMed:33301566). However, other studies suggest that GORASP2 plays a role in the assembly and membrane stacking of the Golgi cisternae, and in the process by which Golgi stacks reform after breakdown during mitosis and meiosis (PubMed:10487747, PubMed:21515684, PubMed:22523075). May regulate the intracellular transport and presentation of a defined set of transmembrane proteins, such as transmembrane TGFA (PubMed:11101516). Required for normal acrosome formation during spermiogenesis and normal male fertility, probably by promoting colocalization of JAM2 and JAM3 at contact sites between germ cells and Sertoli cells (By similarity). Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (PubMed:21884936, PubMed:27062250, PubMed:28067262).

100 Clinical Results associated with GORASP2

100 Translational Medicine associated with GORASP2

0 Patents (Medical) associated with GORASP2

119

Literatures (Medical) associated with GORASP2

17 Mar 2025·The Journal of Clinical Endocrinology & Metabolism

Genetic Associations With C-peptide Levels Before Type 1 Diabetes Diagnosis in At-risk Relatives

Article

Author: Oram, Richard A ; Ferrat, Lauric A ; Onengut-Gumuscu, Suna ; You, Lu ; Tosur, Mustafa ; Rich, Stephen S ; Redondo, Maria J ; Parikh, Hemang M ; Krischer, Jeffrey P ; Triolo, Taylor M ; Steck, Andrea K ; Gottlieb, Peter A

AbstractObjectiveWe sought to determine whether the type 1 diabetes genetic risk score-2 (T1D-GRS2) and single nucleotide polymorphisms are associated with C-peptide preservation before type 1 diabetes diagnosis.MethodsWe conducted a retrospective analysis of 713 autoantibody-positive participants who developed type 1 diabetes in the TrialNet Pathway to Prevention Study who had T1DExomeChip data. We evaluated the relationships of 16 known single nucleotide polymorphisms and T1D-GRS2 with area under the curve (AUC) C-peptide levels during oral glucose tolerance tests conducted in the 9 months before diagnosis.ResultsHigher T1D-GRS2 was associated with lower C-peptide AUC in the 9 months before diagnosis in univariate (β = −.06, P < .0001) and multivariate (β = −.03, P = .005) analyses. Participants with the JAZF1 rs864745 T allele had lower C-peptide AUC in both univariate (β = −.11, P = .002) and multivariate (β = −.06, P = .018) analyses.ConclusionThe type 2 diabetes-associated JAZF1 rs864745 T allele and higher T1D-GRS2 are associated with lower C-peptide AUC before diagnosis of type 1 diabetes, with implications for the design of prevention trials.

01 Mar 2025·Molecular Biology of the Cell

GRASP55 regulates sorting and maturation of the lysosomal enzyme β-hexosaminidase A

Article

Author: Javed, Aadil ; Akaaboune, Sarah Reem ; Wierenga, Alissa ; Wang, Yanzhuang ; Bui, Sarah

The Golgi apparatus plays a crucial role in the delivery of lysosomal enzymes. Golgi reassembly stacking proteins, GRASP55 and GRASP65, are vital for maintaining Golgi structure and function. GRASP55 depletion results in the missorting and secretion of the lysosomal enzyme cathepsin D, though the mechanisms remain unclear. In this study, we conducted secretomic analyses of GRASP55 knockout cells and found a significant increase in lysosome-associated proteins in the extracellular medium. Using the lysosomal beta-hexosaminidase subunit alpha (HEXA) as a model, we found that GRASP55 depletion disrupted normal trafficking and processing of HEXA, resulting in increased secretion of the immature (pro-form) HEXA into the extracellular milieu, along with decreased levels of the mature form and enzymatic activity within the cell. GRASP55 depletion significantly reduced the complex formation between HEXA and mannose 6-phosphate (M6P) receptors (MPR), despite no overall change in MPR expression. Finally, we found there was a notable reduction in the expression of GNPTAB, leading to a reduction in M6P modification of HEXA, hindering its efficient targeting to lysosomes. These findings reveal the role of GRASP55 in regulating lysosomal enzyme dynamics, emphasizing its role in the sorting and trafficking of lysosomal proteins.

01 Feb 2025·Cell Reports

Dendritic cell phagosomes recruit GRASP55 for export of antigen-loaded MHC molecules

Article

Author: Brouwers, Nathalie ; Pena Rodríguez, María Jesús ; Malhotra, Vivek ; Dinamarca, Sofía ; Blanchard, Nicolas ; Cebrian, Ignacio ; Sancho, David ; Barends, Martina ; Priego, Elena ; Brunnberg, Jamina ; Tampé, Robert

Dendritic cells (DCs) present exogenous antigens via major histocompatibility complex class I (MHC-I) and MHC class II (MHC-II) molecules, activating CD8⁺ and CD4⁺ T cells. A critical but poorly understood step in this process is the trafficking of peptide-loaded MHC molecules from the endocytic system to the cell surface. In this study, we demonstrate that the Golgi reassembly-stacking protein of 55 kDa (GRASP55), which has been shown to have no role in stacking, is essential for antigen presentation. Using soluble, bead-coated, and bacterial-bound antigens, we found significantly impaired exogenous antigen presentation in GRASP55-deficient bone-marrow-derived DCs (BMDCs). Notably, GRASP55 was recruited to late phagosomes, and our data suggest that it is crucial for sorting MHC-I and MHC-II molecules, facilitating their trafficking to the plasma membrane. Our findings highlight the vital role of GRASP55 in the intracellular transport of MHC molecules bound to their respective peptides during exogenous antigen presentation.

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GORASP2

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