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Patil, H.

Publications and source records attributed to Patil, H..

2 recordsLinked to original sources

Human activities drive novel behaviours and transitions in dolphins

Intensifying human activities are reshaping coastal ecosystems, yet their impact on wildlife behaviour and survival remain poorly understood. We conducted drone-based focal-group follows of endangered Indian Ocean humpback dolphin groups in Goa, India, to quantify how tourism and fisheries jointly impact behavioural states and transitions. By integrating machine learning and georeferencing techniques, we found that both human activities triggered distinct behavioural transitions absent in undisturbed groups. Dolphins expressed escape behaviours exclusively near tourist boats and were more likely to transition into foraging near fishing nets (mostly purse-seines). Smaller groups reacted more strongly to tourist boats and interacted more frequently with fishing nets, especially in seasons when fish landing data showed a decline in their prey. These findings offer new insights into the behavioural mechanisms underlying the co-occurrence of coastal dolphins with humans and provide broader guidelines for managing tourism and fisheries to reduce anthropogenic pressure on threatened delphinids.

ecology↗

Proteostatic remodeling of small heat shock chaperones - crystallins by Ran-binding protein 2 and the peptidyl-prolyl cis-trans isomerase and chaperone activities of its cyclophilin domain.

Disturbances in phase transitions and intracellular partitions of nucleocytoplasmic shuttling substrates promote protein aggregation - a hallmark of neurodegenerative diseases. The modular Ran-binding protein 2 (Ranbp2) is a cytosolic molecular hub for rate-limiting steps of disassembly and phase transitions of Ran-GTP-bound protein ensembles exiting nuclear pores. Chaperones also play central roles in phase transitions and proteostasis by suppressing protein aggregation. Ranbp2 haploinsufficiency promotes the age-dependent neuroprotection of the chorioretina against photo-oxidative stress by proteostatic regulations of Ranbp2 substrates and by countering the build-up of poly-ubiquitylated substrates. Further, the peptidyl-prolyl cis-trans isomerase (PPIase) and chaperone activities of the cyclophilin domain (CY) of Ranbp2 modulate the proteostasis of selective neuroprotective substrates, such as hnRNPA2B1, STAT3, HDAC4 or L/M-opsin, while promoting a decline of ubiquitylated substrates. However, links between CY PPIase activity on client substrates and its effect(s) on ubiquitylated substrates are unclear. Here, proteomics of genetically modified mice with deficits of Ranbp2 uncovered the regulation of the small heat shock chaperones - crystallins by Ranbp2 in the chorioretina. Loss of CY PPIase of Ranbp2 up-regulates A-crystallin proteostasis, which is repressed in non-lenticular tissues. Conversely, the A-crystallins substrates, {gamma}-crystallins, are down-regulated by impairment of CY s C-terminal chaperone activity. These CY-dependent effects cause the age-dependent decline of ubiquitylated substrates without overt chorioretinal morphological changes. A model emerges whereby the Ranbp2 CY-dependent remodeling of crystallins proteostasis subdues molecular aging and preordains chorioretinal neuroprotection by augmenting the chaperone buffering capacity and the decline of ubiquitylated substrates against proteostatic impairments. Further, CYs moonlighting activity holds pan-therapeutic potential against neurodegeneration.

genetics↗