NucleaRDB: Extraction of mutation data from the literature

2005, NucleaRDB.

This data was extracted from Medline abstracts and full texts (when available) in an automated manner.

The table below describes the selected point mutation and provides links to other documents. The sentence(s) where the point mutation D154N was found are listed after the table.

The mutated residues are also indicated in the family sequence alignments and hyperlinked to the corresponding mutation pages.

Point mutation D154N in ANDR_HUMAN

Point mutation:	D154N
Domain:	N-term
General numbering (NucleaRDB):	-
Protein:	ANDR_HUMAN (AR,DHTR, NR3C)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein	List of mutations in ANDR_HUMAN
Family alignments	3C4 Androgen (AR) 3C Glucocorticoid-like (GR,MR,PR,AR) 3 Estrogen like (ER,ERR,GR,MR,PR,AR)
Other point mutations / same position
Reference:	Kennedy's disease: Phosphorylation of the polyQ-expanded form of androgen receptor regulates its cleavage by caspase-3 and enhances cell death. LaFevre-Bernt MA, Ellerby LM J Biol Chem 2003 Jun 24;.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

D154N

B , mouse motor neuron (MN) hybrid cells were transfected with pcDNA3 , AR12 , AR112 , AR112 (S514A) , and AR112 (D154N) in the presence and absence of 1 然 DHT
Because we have previously reported that the caspase-resistant form of the polyQ-expanded form of AR has reduced cellular toxicity , we compared AR112 (S514A) to AR112 (D154N)
Interestingly , the decreased cytotoxicity of the AR112 (S514A) was similar to that observed for AR112 (D154N) , a caspase-resistant form of AR that cannot generate N-terminal polyQ-containing caspasemediated cleavage products (Fig. 4B )
DHT did not modulate the toxicity of cells expressing AR112 (S514A) or AR112 (D154N)
We previously mapped the 32-kDa product formed by caspase-3 cleavage of AR at aspartic acid 154 in the sequence DEDD (Fig. 5B ) and demonstrated that generation of this polyQ AR fragment is toxic to cells because mutation at this site (D154N) greatly reduces cellular toxicity (9 )
DISCUSSION (image)TOP (image)ABSTRACT (image)INTRODUCTION (image)EXPERIMENTAL PROCEDURES (image)RESULTS (image)DISCUSSION (image)REFERENCES The major findings of our studies are (i) AR112 leads to at least a 2-fold increase in phospho-p44 / 42 , -JNK , and -p38 ; (ii) the MEK1 / 2 inhibitor , U0126 , suppresses AR112-induced caspase activation and cell death ; (iii) the phosphorylation of AR is repeat-dependent with increasing phosphorylation occurring with increasing polyQ length ; (iv) mutation in the putative proline-directed phosphorylation site , Ser-514 , blocks AR gel motility and reactivity to serine phospho-specific antibody ; and (v) mutation of Ser-514 in AR112 blocks AR-induced cell death , and the reduction in cellular toxicity is similar to that found for AR112 D154N , a form of AR resistant to caspase cleavage

F.Horn (nucleardbcmbi.kun.nl), 21-Apr-2005