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The protein phosphatase with EF-hand...

Ramulu, Pradeep Y.

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The protein phosphatase with EF-hand family: Biochemical characterization and targeted deletion in mice.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	The protein phosphatase with EF-hand family: Biochemical characterization and targeted deletion in mice./
作者:	Ramulu, Pradeep Y.
面頁冊數:	209 p.
附註:	Adviser: Jeremy Nathans.
Contained By:	Dissertation Abstracts International63-03B.
標題:	Biology, Genetics. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3046541
ISBN:	0493607315

The protein phosphatase with EF-hand family: Biochemical characterization and targeted deletion in mice.
Ramulu, Pradeep Y.

The protein phosphatase with EF-hand family: Biochemical characterization and targeted deletion in mice. - 209 p.

Adviser: Jeremy Nathans.

Thesis (Ph.D.)--The Johns Hopkins University, 2002.

The rdgC/PPEF family of serine/threonine protein phosphatases is distinguished by the presence of C-terminal EF-hands and by neuron-specific expression, including frequent expression in primary sensory neurons. Aside from <italic> Drosophila</italic>, in which mutations in the <italic>rdgC</italic> gene have been demonstrated to cause a light-dependent retinal degeneration due to overphosphorylation of rhodopsin, the functions of the PPEF family are not known. Here we use the <italic>C. elegans</italic> PPEF homolog, CePPEF, as a model for the biochemical characterization of the PPEF family, and undergo the targeted deletion of <italic>PPEF-1</italic> and <italic>PPEF-2</italic> in mouse to understand the function of the PPEF family in vertebrate biology. We demonstrate that CePPEF is N-terminally modified by myristate and palmitate and that it has functional calcium-binding EF-hands at their C-termini. We also show that CePPEF, like other members of the rdgC/PPEF family, is specific to the nervous system and is found in some primary sensory neurons. These primary sensory neurons include the ciliary chemosensory neurons AWB and AWC, and within these cells CePPEF is highly enriched in the sensory cilia. These results establish the first direct evidence for fatty acylation and calcium binding of a PPEF family member and they reveal a remarkable conservation of sensory neuron expression among the members of this distinctive family of protein phosphatases. Targeted deletion of <italic>PPEF-1</italic> and <italic> PPEF-2</italic> in mice demonstrates that PPEF function is not critical for the prevention of retinal degeneration in vertebrates. Moreover, rhodopsin dephosphorylation kinetics are normal in <italic>PPEF-1</italic>/<italic> PPEF-2</italic> double knockouts, suggesting that the PPEFs have a role other than rhodopsin dephosphorylation in vertebrates. The finding that PPEF-2, but not rdgC, has a consensus 14-3-3 binding domain and that PPEF-2 interacts with 14-3-3ζ <italic>in vivo</italic> suggests that PPEF-2 may have a novel role in vertebrate photoreceptors, or that rdgC has a second, unknown function in <italic>Drosophila</italic> photoreceptors which is shared by PPEF-2 and which is uniquely regulated in vertebrates by 14-3-3 association.

ISBN: 0493607315Subjects--Topical Terms:

1017730
Biology, Genetics.

The protein phosphatase with EF-hand family: Biochemical characterization and targeted deletion in mice.
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520 $a The rdgC/PPEF family of serine/threonine protein phosphatases is distinguished by the presence of C-terminal EF-hands and by neuron-specific expression, including frequent expression in primary sensory neurons. Aside from <italic> Drosophila</italic>, in which mutations in the <italic>rdgC</italic> gene have been demonstrated to cause a light-dependent retinal degeneration due to overphosphorylation of rhodopsin, the functions of the PPEF family are not known. Here we use the <italic>C. elegans</italic> PPEF homolog, CePPEF, as a model for the biochemical characterization of the PPEF family, and undergo the targeted deletion of <italic>PPEF-1</italic> and <italic>PPEF-2</italic> in mouse to understand the function of the PPEF family in vertebrate biology. We demonstrate that CePPEF is N-terminally modified by myristate and palmitate and that it has functional calcium-binding EF-hands at their C-termini. We also show that CePPEF, like other members of the rdgC/PPEF family, is specific to the nervous system and is found in some primary sensory neurons. These primary sensory neurons include the ciliary chemosensory neurons AWB and AWC, and within these cells CePPEF is highly enriched in the sensory cilia. These results establish the first direct evidence for fatty acylation and calcium binding of a PPEF family member and they reveal a remarkable conservation of sensory neuron expression among the members of this distinctive family of protein phosphatases. Targeted deletion of <italic>PPEF-1</italic> and <italic> PPEF-2</italic> in mice demonstrates that PPEF function is not critical for the prevention of retinal degeneration in vertebrates. Moreover, rhodopsin dephosphorylation kinetics are normal in <italic>PPEF-1</italic>/<italic> PPEF-2</italic> double knockouts, suggesting that the PPEFs have a role other than rhodopsin dephosphorylation in vertebrates. The finding that PPEF-2, but not rdgC, has a consensus 14-3-3 binding domain and that PPEF-2 interacts with 14-3-3ζ <italic>in vivo</italic> suggests that PPEF-2 may have a novel role in vertebrate photoreceptors, or that rdgC has a second, unknown function in <italic>Drosophila</italic> photoreceptors which is shared by PPEF-2 and which is uniquely regulated in vertebrates by 14-3-3 association.
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