bims-meglyc 2026-02-22 papers

Issue of 2026–02–22
four papers selected by
Silvia Radenkovic, UMC Utrecht

Mol Genet Metab. 2026 Feb 10. pii: S1096-7192(26)00129-0. [Epub ahead of print]147(4): 109846

Albumin as a glycoprotein biomarker in congenital disorders of glycosylation.

Kishore Garapati, Anu Jain, Neha Joshi, Gunveen S Sachdeva, Dowoon Nam, Mayank Saraswat, Raghavendra Rao Pasupuleti, Matthew J Schultz, Tamas Kozicz, Eva Morava, Akhilesh Pandey.

Congenital disorders of glycosylation (CDG) are rare inherited disorders resulting from defects in cellular glycosylation machinery. Albumin has recently been shown to be N-glycosylated at two non-canonical glycosylation sites. We applied multiplexed mass spectrometry-based glycoproteomics to identify site-specific N-glycosylation alterations in albumin from patients with PMM2-CDG, MPI-CDG, SRD5A3-CDG, MAN1B1-CDG and PGM1-CDG. Our findings demonstrate that the glycosylation of albumin is indeed affected in CDG and indicate a potential role for albumin-derived glycopeptides as diagnostic biomarkers.

Keywords: Blood-based biomarkers; Genetic disorders; Glycosylation; HSA; Rare disease diagnosis

DOI: https://doi.org/10.1016/j.ymgme.2026.109846

Subcell Biochem. 2026 ;111 133-176

COG Complex in Golgi Trafficking and Glycosylation.

Farhana Taher Sumya, Vladimir V Lupashin.

The Conserved Oligomeric Golgi (COG) complex, an evolutionary conserved octameric vesicular tether, is essential for maintaining Golgi function by ensuring accurate delivery of resident proteins to their specific locations. Mutations in human COG subunits result in severe multi-systemic diseases known as COG-Congenital Disorders of Glycosylation (COG-CDG). This review explores the current knowledge of COG complex structure, its dynamic behavior, interactions with partner proteins, and proposed models of its cellular functions. Furthermore, we will discuss the pathological implications of mutations in COG complex subunits, as observed in model organisms and human patients.

Keywords: Congenital disorders of glycosylation; Golgi; SNARE; Vesicle tethering; COG

DOI: https://doi.org/10.1007/978-3-032-16833-7_7

Subcell Biochem. 2026 ;111 221-249

Siamese Twins: The Multimodular Mechanisms of Golgi Maturation and Glycan Synthesis Are Coupled at Their Core.

Domenico Russo, Seetharaman Parashuraman, Alberto Luini.

The Golgi apparatus functions as the central processing hub for proteins and lipids, orchestrating glycosylation, sorting, and secretion. Once viewed as a passive site of bulk enzyme recycling, the Golgi is now recognized as a highly dynamic, multimodular system in which intra-Golgi trafficking and glycan synthesis operate as tightly interdependent "Siamese twins." The classical cisternal maturation model, initially based on uniform COPI-mediated recycling, has evolved into the multimodular cisternal maturation (MCM) framework, revealing the coexistence of multiple, specialized recycling modules. Distinct sets of glycosyltransferases form coherent enzymatic modules, each maintained by dedicated retrograde pathways-some COPI-dependent, others COPI-independent-that ensure compartmental fidelity and enable differential regulation of glycan synthesis. These pathways are coordinated by adaptors, retainers, and lipid identity cues that collectively sustain Golgi polarity and adaptability to cellular and metabolic states. Disruption of this modular recycling logic leads to enzyme mislocalization, defective glycosylation, and disease, ranging from congenital disorders of glycosylation to oncogenic transformation. The transition from bulk to multimodular recycling thus redefines the Golgi as an integrated regulatory platform linking membrane trafficking to metabolic and signaling networks.

Keywords: Cancer; Cisternal maturation; Congenital disorders of glycosylation; Glycosylation; Multimodular recycling; Golgi apparatus

DOI: https://doi.org/10.1007/978-3-032-16833-7_10

Biochim Biophys Acta Gen Subj. 2026 Feb 18. pii: S0304-4165(26)00019-X. [Epub ahead of print]1870(5): 130919

Impact of Golgi dynamics and Golgi morphology on the regulation of glycosylation.

Paul A Gleeson.

The Golgi apparatus is a highly dynamic organelle and central to the regulation of protein glycosylation, cargo sorting and additional cellular processes such as mitosis, stress responses, autophagy and inflammation. There have been major advances in understanding the dynamics of the Golgi apparatus and the relationship between remodelling the Golgi architecture and function. Membrane structural/scaffold proteins of the Golgi, including golgins, GRASPs and adaptors interact with a diverse range of cytoskeletal and signalling molecules and play a major role in the regulation of the Golgi morphology and function. Modulation of the higher-order Golgi ribbon architecture in mammalian cells is directly associated with physiological and pathological responses, including neurological diseases and cancer. An important question is the influence of morphological states of the Golgi architecture on the fine tuning of glycosylation. Here we review the relationship between the morphology and function of this organelle, in physiology and disease, especially to in relation to the impact of the fragmentation of the Golgi ribbon on the steady state location of glycosyltransferases and glycan synthesis. The current unresolved issues relevant to changes in Golgi morphology on protein glycosylation are highlighted.

Keywords: Actin; Glycan synthesis; Glycosyltransferase; Golgi morphology; Golgi ribbon; Microtubules; Signaling

DOI: https://doi.org/10.1016/j.bbagen.2026.130919