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Biology subjects

Lieu, E. C.

Publications and source records attributed to Lieu, E. C..

2 recordsLinked to original sources

Intracellular Mechanosensation in Intestinal Smooth Muscle: Piezo1 Complexes Amplify Signaling Beyond the Surface

Mechanosensation is fundamentally viewed as a plasma membrane phenomenon. We challenge this paradigm by introducing intracellular mechanosensation in intestinal smooth muscle. We hypothesized that a distinct, organelle-based signaling axis exists to amplify mechanotransduction from the inside out. To test this, we investigated whether Piezo1, a canonical plasma membrane mechanosensor, also operates within the cell. Using tissue-level wire myography, high-resolution confocal microscopy, proximity ligation assays, and patch-clamp electrophysiology on freshly dissociated cells, we identified a functional intracellular signaling hub that starts at the sarcoplasmic reticulum (SR). Unlike surface transduction, this intracellular mechanism relies on a nanoscale multiprotein complex (<40 nm) comprising an SR sensor (intra-Piezo1) and an amplifier (Ryanodine Receptor, RyR), coupled with a PM effector (large-conductance, Ca2+-activated K+ channels, i.e., BKCa channels). Activating this intracellular complex generated massive BK-mediated outward currents independent of extracellular Ca{superscript 2} but strictly dependent on internal SR Ca{superscript 2} stores, confirming intrinsic organellar mechanotransduction. Within this complex, intra-Piezo1 and RyR are positioned to operate as a coupled SR Ca{superscript 2} release unit that activates BK channels at SR-PM junctions, driving potent membrane hyperpolarization that reduces smooth muscle contractility, revealing the intra-Piezo1 complex as a molecular brake on excitation. These findings demonstrate that mechanotransduction is not confined to the cell surface. Instead, a specialized Sensor-Amplifier-Effector complex originating at intracellular organelles amplifies cellular sensitivity to physical force, providing a critical gain-control system that restrains smooth muscle excitability and regulates GI motility. Key PointsO_LIIntracellular organelles contribute to mechanosensory signaling in GI smooth muscle cells, complementing plasma membrane mechanisms. C_LIO_LIIntra-Piezo1 form a nanoscale signaling complex (<40nm) on the sarcoplasmic reticulum (SR), linking the mechanosensor Piezo1 with RyR and large conductance, Ca2+-activated K+ channels. C_LIO_LIUnlike surface sensors, this intracellular complex functions via a "Sensor-Amplifier-Effector" mechanism in which intra-Piezo1 detects mechanical stress and triggers SR Ca2+ release, thereby activating a nearby RyR and large-conductance, Ca2+-activated K+ channel. C_LIO_LIEngaging this intracellular Piezo1-mediated axis significantly dampens smooth muscle contractility, identifying a critical gain-control system essential for regulating GI motility. C_LI

physiology↗

The GARP Domain of the Rod CNG Channel's β1-subunit Contains Distinct Sites for Outer Segment Targeting and Connecting to the Photoreceptor Disc Rim

Vision begins when light is captured by the outer segment organelle of photoreceptor cells in the retina. Outer segments are modified cilia filled with hundreds of flattened disc-shaped membranes. Disc membranes are separated from the surrounding plasma membrane and each membrane type has unique protein components. The mechanisms underlying this protein sorting remain entirely unknown. In this study, we investigated the outer segment delivery of the rod cyclic nucleotide-gated (CNG) channel, which is located in the outer segment plasma membrane where it mediates the electrical response to light. We now show that the targeted delivery of the CNG channel to the outer segment requires pre-assembly of its constituent 1 and {beta}1 subunits and that CNG{beta}1 contains specific targeting information encoded within the glutamic acid-rich region of its N-terminal GARP domain. We also found that the GARP domain connects the CNG channel to photoreceptor disc rims likely through an interaction with peripherin-2 and demonstrated that this function is performed by a proline-enriched region adjacent to the GARP domain. Our data reveal fine functional specializations within the structural domains of the CNG channel and suggest that channel delivery to the outer segment is independent of peripherin-2 interactions. Significance StatementThe precise delivery and organization of signaling proteins in the ciliary outer segment organelle of photoreceptor cells is critical for light detection. We report that the CNG channel, mediating the electrical response to light in rods, contains a region within the N-terminus of its CNG{beta}1 subunit that encodes the outer segment targeting information for the entire channel. This targeting region is adjacent to a region that connects CNG{beta}1 to the rims of photoreceptor discs, likely determining the subcellular compartmentalization of the CNG channel into the outer segment plasma membrane.

cell biology↗