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Chen, C.-X.

Publications and source records attributed to Chen, C.-X..

2 recordsLinked to original sources

Continuous flashing suppression of V1 responses and the perceptual consequences revealed via two-photon calcium imaging and transformer modeling

Continuous flash suppression (CFS), a dynamic masker presented to one eye suppressing the conscious perception of a stimulus shown to the other eye, has been extensively used to study visual consciousness. Various studies reported high-level visual and cognitive functions under CFS, which, however, has more recently been questioned and at least partially attributed to low-level stimulus properties. A key but unsettled issue is the extent to which the responses of V1 neurons, where inputs from two eyes first merge, are affected, as severely suppressed V1 responses would not sustain high-level processing. Here, we used two-photon calcium imaging to record the responses of large samples of V1 neurons to a grating stimulus under CFS in awake, fixating macaques. The results revealed that CFS substantially suppressed V1 orientation responses. Ocularity-wise, it nearly completely eliminated the orientation responses of V1 neurons preferring the masker eye or both eyes, while also significantly suppressing the responses of those preferring the grating eye. Modeling analyses suggest that, under CFS, the brain retains the ability of classifying coarse orientations, but may become less capable of reconstructing the grating stimulus. Consequently, while CFS-suppressed orientation information still supports low-level orientation discrimination, it may not suffice for high-level visual and cognitive processing.

neuroscience↗

Coupling of H3K27me3 recognition with transcriptional repression through the BAH-PHD-CPL2 complex in Arabidopsis

Histone 3 Lys 27 trimethylation (H3K27me3)-mediated epigenetic silencing plays a critical role in multiple biological processes. However, the H3K27me3 recognition and transcriptional repression mechanisms are only partially understood. Here, we report a new mechanism for H3K27me3 recognition and transcriptional repression. Our structural and biochemical data showed that the BAH domain protein AIPP3 and the PHD proteins AIPP2 and PAIPP2 cooperate to read H3K27me3 and unmodified H3K4 histone marks, respectively, in Arabidopsis. The BAH-PHD bivalent histone reader complex silences a substantial subset of H3K27me3-enriched loci, including a number of development and stress response-related genes such as the RNA silencing effector gene ARGONAUTE 5 (AGO5) and We found that the BAH-PHD module associates with CPL2, a plant-specific Pol II carboxyl terminal domain (CTD) phosphatase, to form the BAH-PHD-CPL2 complex (BPC) for transcriptional repression. The BPC complex represses transcription through CPL2-mediated CTD dephosphorylation, thereby causing inhibition of Pol II release from the transcriptional start site. Our work reveals a mechanism coupling H3K27me3 recognition with transcriptional repression through the alteration of Pol II phosphorylation states, thereby contributing to our understanding of the mechanism of H3K27me3-dependent silencing.

plant biology↗