Publications by authors named "Maciej Jagielnicki"
Article Synopsis
- Connexins (Cxs) are integral membrane proteins that form hemichannels and gap junctions, enabling communication between cells and their environment, which is vital for development and response to diseases.
- Abnormal functioning of these channels can lead to various health issues, including inflammation, skin diseases, deafness, and heart problems.
- Recent studies using high-resolution imaging techniques have revealed detailed structures of Cxs, uncovering mechanisms of channel regulation and potential future research directions to explore their functions in cellular communication.
Surface lipoproteins (SLPs) are peripherally attached to the outer leaflet of the outer membrane in many Gram-negative bacteria, playing significant roles in nutrient acquisition and immune evasion in the host. While the factors that are involved in the synthesis and delivery of SLPs in the inner membrane are well characterized, the molecular machinery required for the movement of SLPs to the surface are still not fully elucidated. In this study, we investigated the translocation of a SLP TbpB through a Slam1-dependent pathway.
View Article and Find Full Text PDFThe human zinc transporter ZnT8 (SLC30A8) is expressed primarily in pancreatic β-cells and plays a key function in maintaining the concentration of blood glucose through its role in insulin storage, maturation and secretion. ZnT8 is an autoantigen for Type 1 diabetes (T1D) and is associated with Type 2 diabetes (T2D) through its risk allele that encodes a major non-synonymous single nucleotide polymorphism (SNP) at Arg325. Loss of function mutations improve insulin secretion and are protective against diabetes.
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- Connexins (Cx) form gap junction channels (GJCs) by creating hexameric hemichannels that connect adjacent cells, allowing for cell-to-cell communication and independent transport of substances in and out of the cells.
- A mutation (N176Y) was introduced in Cx26, enabling researchers to analyze the structure of these hemichannels using electron cryomicroscopy, revealing an open pore design similar to GJCs.
- The study highlights the importance of the conformational flexibility of extracellular loops in recognizing compatible connexin isoforms for effective intercellular docking, while also linking these findings to past research on the function and properties of connexin hemichannels.
Gap junction channels (GJCs) mediate intercellular communication and are gated by numerous conditions such as pH. The electron cryomicroscopy (cryo-EM) structure of Cx26 GJC at physiological pH recapitulates previous GJC structures in lipid bilayers. At pH 6.
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