The MinK Potassium Channel Exists in Functional and Nonfunctional Forms When Expressed in the Plasma Membrane of \u3cem\u3eXenopus\u3c/em\u3e Oocytes

The minK protein induces a slowly activating voltage-dependent potassium current when expressed in Xenopus oocytes. In order to measure the levels of minK protein in the plasma membrane, we have modified the minK gene by inserting a 9 amino acid epitope into the N- terminal domain of the protein sequence. When intact live oocytes are injected with the modified minK RNA and subsequently incubated with an antibody to this epitope, specific binding is detected, indicating that the N-terminal domain is extracellular. We found that when oocytes are injected with amounts of minK mRNA up to 50 ng, the levels of protein at the surface are proportional to the amount of injected mRNA. In contrast, the amplitude of the minK current recorded in the oocytes saturates at 1 ng of injected mRNA. Although the amplitude of the currents is not altered by increasing mRNA levels above 1 ng, the kinetics of activation of the current differ in oocytes with high or low levels of minK RNA. In particular, activation is slower with higher levels of minK protein in the plasma membrane. Finally, we find that increasing intracellular cAMP levels, which increases the amplitude of minK currents, does not alter surface expression of the minK protein but produces a small increase in the rate of activation of the current. Our results support a model in which minK protein forms functional potassium channels by association with a factor endogenous to the oocyte

Wetland Types

This resource will help students to distinguish between wetland types. They will discover that coastal wetlands include salt marshes and tidal brackish marshes while inland wetlands consist of freshwater marshes, wet meadows, forested swamps, shrub swamps, bogs, fens, and vernal pools. A Guide to Wetland Wildlife in New England Regional Wetland "Celebrities" is included. This site is part of a guide that aims to help students get to know the complexities of wetlands, discover wildlife, enjoy the experience of being outdoors, and learn how necessary wetlands are to the health of our environment. Even though the site is about wetlands in New England for educators and their middle school students it suggests ways to study wetland characteristics, why wetlands are important, and how students and teachers can help protect a local wetland. An associated set of activities is also available. Educational levels: Middle school

The conduction pore of a cardiac potassium channel.

Ion channels form transmembrane water-filled pores that allow ions to cross membranes in a rapid and selective fashion. The amino acid residues that line these pores have been sought to reveal the mechanisms of ion conduction and selectivity. The pore (P) loop is a stretch of residues that influences single-channel-current amplitude, selectivity among ions and open-channel blockade and is conserved in potassium-channel subunits previously recognized to contribute to pore formation. To date, potassium-channel pores have been shown to form by symmetrical alignment of four P loops around a central conduction pathway. Here we show that the selectivity-determining pore region of the voltage-gated potassium channel of human heart through which the I(Ks) current passes includes the transmembrane segment of the non-P-loop protein minK. Two adjacent residues in this segment of minK are exposed in the pore on either side of a short barrier that restricts the movement of sodium, cadmium and zinc ions across the membrane. Thus, potassium-selective pores are not restricted to P loops or a strict P-loop geometry

Modulation by cAMP of a Slowly Activating Potassium Channel Expressed in \u3cem\u3eXenopus\u3c/em\u3e Oocytes

When expressed in the Xenopus oocyte, the minK protein induces a slowly activating voltage-dependent potassium current (Isk). We studied the modulation of this current by altering intracellular cAMP levels and found that the amplitude of Isk is dramatically increased by treatments that raise cAMP levels and decreased by agents that lower cAMP levels. Preinjection of a protein inhibitor of the cAMP-dependent protein kinase blocked the effects of increased cAMP levels. There were no changes in the voltage dependence or kinetics of Isk. Mutations that eliminate a potential phosphorylation site on the minK protein did not block the effects of activating the kinase. In addition, the membrane capacitance of the oocyte increased and decreased in parallel with Isk. Our results fit a mechanism in which channel proteins are selectively inserted into and removed from the plasma membrane in response to changes in kinase activity

Relations of environmental contaminants, algal toxins, and diet with the reproductive success of American alligators on Florida Lakes

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NEW AND UPDATED RECORDS FOR AMPHIBIANS AND REPTILES IN MINNESOTA, USA

Following the publication of the revised edition of “Amphibians and Reptiles in Minnesota” by Moriarty and Hall (2014), we accessioned several new or updated records at the Bell Museum of Natural History (JFBM). Records include digital photographs (accession number preceded by “P”) and audio recordings (accession number preceded by “AUD”). In addition, a subset of these observations were accessioned in www.HerpMapper.org. HerpMapper accession numbers are preceded by “HM” and can be viewed online. Benjamin Lowe verified species determinations. Latitude and longitude coordinates are based on datum WGS 84

MiRP2 forms potassium channels in skeletal muscle with Kv3.4 and is associated with periodic paralysis.

The subthreshold, voltage-gated potassium channel of skeletal muscle is shown to contain MinK-related peptide 2 (MiRP2) and the pore-forming subunit Kv3.4. MiRP2-Kv3.4 channels differ from Kv3.4 channels in unitary conductance, voltage-dependent activation, recovery from inactivation, steady-state open probability, and block by a peptide toxin. Thus, MiRP2-Kv3.4 channels set resting membrane potential (RMP) and do not produce afterhyperpolarization or cumulative inactivation to limit action potential frequency. A missense mutation is identified in the gene for MiRP2 (KCNE3) in two families with periodic paralysis and found to segregate with the disease. Mutant MiRP2-Kv3.4 complexes exhibit reduced current density and diminished capacity to set RMP. Thus, MiRP2 operates with a classical potassium channel subunit to govern skeletal muscle function and pathophysiology

Biological Assessments of Six Selected Fishes, Amphibians, and Mussels in Illinois

ID: 8758; issued November 1, 1996INHS Technical Report prepared for Illinois Department of Natural Resources, Division of Natural Heritag