TY - JOUR
T1 - Generation and Characterization of LANP/pp32 Null Mice
AU - Opal, Puncet
AU - Garcia, Jesus J.
AU - McCall, Alanna E.
AU - Xu, Bisong
AU - Weeber, Edwin J.
AU - Sweatt, J. David
AU - Orr, Harry T.
AU - Zoghbi, Huda Y.
PY - 2004/4
Y1 - 2004/4
N2 - The leucine-rich acidic nuclear protein (LANP) belongs to a family of evolutionarily conserved proteins that are characterized by an amino-terminal domain rich in leucine residues followed by a carboxy-terminal acidic tail. LANP has been implicated in the regulation of a variety of cellular processes including RNA transport, transcription, apoptosis, vesicular trafficking, and intracellular signaling. Abundantly expressed in the developing cerebellum, this protein has also been hypothesized to play a role in cerebellar morphogenesis. LANP has been implicated in disease biology as well, both as a mediator of toxicity in spinocerebellar ataxia type 1 and as a tumor suppressor in cancers of the breast and prostate. To better understand the function of this multifaceted protein, we have generated mice lacking LANP. Surprisingly, these mice are viable and fertile. In addition we could not discern any derangements in any of the major organ systems, including the nervous system, which we have studied in detail. Overall our results point to a functional redundancy of LANP's function, most likely provided by its closely related family members.
AB - The leucine-rich acidic nuclear protein (LANP) belongs to a family of evolutionarily conserved proteins that are characterized by an amino-terminal domain rich in leucine residues followed by a carboxy-terminal acidic tail. LANP has been implicated in the regulation of a variety of cellular processes including RNA transport, transcription, apoptosis, vesicular trafficking, and intracellular signaling. Abundantly expressed in the developing cerebellum, this protein has also been hypothesized to play a role in cerebellar morphogenesis. LANP has been implicated in disease biology as well, both as a mediator of toxicity in spinocerebellar ataxia type 1 and as a tumor suppressor in cancers of the breast and prostate. To better understand the function of this multifaceted protein, we have generated mice lacking LANP. Surprisingly, these mice are viable and fertile. In addition we could not discern any derangements in any of the major organ systems, including the nervous system, which we have studied in detail. Overall our results point to a functional redundancy of LANP's function, most likely provided by its closely related family members.
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U2 - 10.1128/MCB.24.8.3140-3149.2004
DO - 10.1128/MCB.24.8.3140-3149.2004
M3 - Article
C2 - 15060138
AN - SCOPUS:1842557732
SN - 0270-7306
VL - 24
SP - 3140
EP - 3149
JO - Molecular and cellular biology
JF - Molecular and cellular biology
IS - 8
ER -