Efficient single-photon detection by retinal rod photoreceptors requires timely and reproducible deactivation of rhodopsin. Like other G protein-coupled receptors, rhodopsin contains multiple sites for phosphorylation at its COOH-terminal domain. Transgenic and electrophysiological methods were used to functionally dissect the role of the multiple phosphorylation sites during deactivation of rhodopsin in intact mouse rods. Mutant rhodopsins bearing zero, one (S338), or two (S334/S338) phosphorylation sites generated single-photon responses with greatly prolonged, exponentially distributed durations. Responses from rods expressing mutant rhodopsins bearing more than two phosphorylation sites declined along smooth, reproducible time courses; the rate of recovery increased with increasing numbers of phosphorylation sites. We conclude that multiple phosphorylation of rhodopsin is necessary for rapid and reproducible deactivation.

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Existing multicast routing mechanisms were intended for use within regions where a group is widely represented or bandwidth is universally plentiful. When group members, and senders to those group members, are distributed sparsely across a wide area, these schemes are not efficient; data packets or membership report information are occasionally sent over many links that do not lead to receivers or senders, respectively. We have developed a multicast routing architecture that efficiently establishes distribution trees across wide area internets, where many groups will be sparsely represented. Efficiency is measured in terms of the state, control message processing, and data packet processing, required across the entire network in order to deliver data packets to the members of the group. Our Protocol Independent Multicast (PIM) architecture: (a) maintains the traditional IP multicast service model of receiver-initiated membership; (b) can be configured to adapt to different multicast group and network characteristics; (c) is not dependent on a specific unicast routing protocol; and (d) uses soft-state mechanisms to adapt to underlying network conditions and group dynamics. The robustness, flexibility, and scaling properties of this architecture make it well suited to large heterogeneous inter-networks.

Background: Mitotic progression is regulated by reversible protein phosphorylation involving kinases and phosphatases. Results: Pnuts functions as a master regulator of mitosis by modulating PP1; Pnuts expression peaks in mitosis and is degraded at mitotic exit. Conclusion: This study reveals the function and regulation of a new and essential mitotic regulator. Significance: This study improves our understanding of M-phase regulation.