bims-lycede Biomed News
on Lysosome-dependent cell death
Issue of 2026–05–10
two papers selected by
Sofía Peralta, Universidad Nacional de Cuyo
  1. Endoplasmic reticulum and Golgi stress signaling-mediated regulation of protein secretion.
  2. Membrane Protein Glycosylation Revisited: Functional Dynamics and Emerging Clinical Insights.
  1. Cell Mol Biol Lett. 2026 May 07.
    Endoplasmic reticulum and Golgi stress signaling-mediated regulation of protein secretion.
    Ketsia Bakambamba, Manon Nivet, Sophie Martin, Elodie Lafont, Eric Chevet, Tony Avril.
      The eukaryotic secretory pathway (SP) is essential to ensure cellular functions and multicellular communication. The early SP is constituted mostly of the endoplasmic reticulum (ER), the ER-Golgi intermediate compartment (ERGIC), and the Golgi apparatus. These intracellular organelles achieve proper folding and modification of newly synthesized transmembrane and secretory proteins, en route to their final destination, e.g., plasma membrane, endosomes, lysosomes, and the extracellular space. They also integrate quality control systems to ensure export of productively folded proteins and to trigger dysfunctional proteins to degradation. The ER as the first SP compartment is subjected to a precise control of its own homeostasis through signaling of the unfolded protein response. In this review, we provide an overview of the early SP and its regulatory mechanisms, focusing on the ER and Golgi stress-dependent signaling. We contextualize this information within physiological and pathological processes, and discuss how ER and Golgi stress responses might coordinate their regulatory effects across the entire SP.
    Keywords:  Endoplasmic reticulum stress response; Golgi stress response; Protein secretion machinery; Secretory pathway
    DOI:  https://doi.org/10.1186/s11658-026-00932-w
  2. Int J Mol Sci. 2026 Apr 16. pii: 3575. [Epub ahead of print]27(8):
    Membrane Protein Glycosylation Revisited: Functional Dynamics and Emerging Clinical Insights.
    Kyung-Hee Kim, Byong Chul Yoo.
      Glycosylation is one of the most prevalent post-translational modifications of membrane proteins and plays a central role in regulating their structure and function. Unlike many existing reviews that address glycosylation in a system-wide context, this review focuses specifically on membrane proteins and examines how glycosylation shapes their functional behavior and clinical relevance. Because membrane proteins are exposed to the extracellular environment, glycans on their surface directly influence protein folding, receptor organization, and interactions with ligands and immune components. These diverse effects can be understood within a common mechanistic framework in which glycosylation modulates protein conformation, receptor clustering, and membrane organization, thereby altering signaling, adhesion, transport, and immune recognition. We discuss how N-linked and O-linked glycosylation regulate major classes of membrane proteins across these processes. Particular attention is given to disease-associated alterations in glycosylation, especially in cancer, immune and inflammatory disorders, and metabolic disease. For instance, glycosylation-dependent stabilization of PD-L1 and modulation of receptor signaling, such as EGFR, illustrate how glycan modifications contribute to immune evasion and therapeutic response. We further consider the clinical implications of membrane protein glycosylation, including its roles in biomarker development and as a potential target for therapeutic intervention. Advances in glycoproteomic technologies have enabled increasingly detailed characterization of site-specific glycosylation, although significant analytical challenges remain, particularly for membrane proteins. Overall, this review highlights membrane protein glycosylation as a dynamic regulatory layer that links molecular mechanisms to functional outcomes and clinical applications.
    Keywords:  N-linked glycans; clinical translation; glycoproteomics; glycosylation; membrane proteins
    DOI:  https://doi.org/10.3390/ijms27083575
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