Polycystin-L is a calcium-regulated cation channel permeable to calcium ions
Article Abstract:
It has been established that polycystin-L, which is deleted in mice with renal and retinal defects, is a calcium-modulated nonselective cation ion channel. It is permeable to potassium, sodium and calcium ions. It is distinguished from structurally related channels of the TRP family, voltage-gated Ca2+ and Na+ channels and known endogenous cation channels in Xenopus oocytes by its ion selectivity, relatively long open time and large single-channel conductance. There are structural similarities between polycystin-L and polycystin-2, and it is likely that both have channel properties.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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Primary structure and functional characterization of a high-affinity glutamate transporter
Article Abstract:
The genetic basis and physiological role of a glutamate transporter has been determined. Glutamate transport, which is an important part of neurotransmission, results from a protein generated by a newly cloned form of complementary DNA. This 524 amino acid protein has been designated the excitatory amino acid carrier (EAAC1). EAAC1 causes the glutamate transporter to rely on sodium ions but not on chlorine ions to effect transport through cellular membranes. This protein's malfunctioning may underlie the neurodegenerative diseases linked to abnormal glutamate transport.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
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Rim is a putative Rab3 effector in regulating synaptic-vesicle fusion
Article Abstract:
It has been possible to identify a putative Rab3-effector protein made up of an amino-terminal zinc-finger motif and carboxy-terminal PDZ and C2 domains. This protein, known as Rim, binds only to GTP-complexed Rab3. Both Rim and rabphilin have C2 domains, but those of Rim occur in a different domain context and are structurally distinct. This distinguishes Rim from the vesicular C2 domain proteins rabphilin and synaptotagmins. Rim is only found on presynaptic active zones and synaptic ribbons.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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