ypandit
commented
10 years ago Input:
<summary paragraph_no="3782">The <i>abpA</i> gene encodes alpha-actinin, a 95 kD protein originally isolated from the cell cortex. It forms a dimer, crosslinks actin filaments (<a href="/ontology/go/0051017/annotation/page/1">actin filament bundle formation</a>) into lateral arrays, and increases the actin-stimulated Mg ATPase of myosin. Both activities are regulated by Ca2+ <a href="http://www.ncbi.nlm.nih.gov/pubmed/6746725"> (Condeelis et al. 1984)</a>. The alpha-actinin molecule carries two characteristic EF-hand structures. The calcium-binding loops form the structural basis for the calcium sensitivity (<a href="/ontology/go/0005509/annotation/page/1">calcium ion binding</a>) <a href="http://www.ncbi.nlm.nih.gov/pubmed/3622778"> (Noegel et al. 1987)</a>. It was shown that EF hand I has a low affinity for Ca2+ and EF hand II a high affinity, implying a regulatory function of EF hand I in the inhibition of F-actin cross-linking activity <a href="http://www.ncbi.nlm.nih.gov/pubmed/8486739"> (Witke et al. 1993)</a>. This was confirmed when the viscoelastic properties of F-actin solutions in the presence of mutated EF hand structures was tested, and it was concluded that the first EF hand of alpha-actinin is crucial for its crosslinking function <a href="http://www.ncbi.nlm.nih.gov/pubmed/8561496"> (Janssen et al. 1996)</a>.<br/>The phenotype of an alpha-actinin mutant, HG1130, which retained only trace amounts of alpha-actinin, appeared to be normal <a href="http://www.ncbi.nlm.nih.gov/pubmed/3956480"> (Wallraff et al. 1986)</a>. The lack of alpha-actinin was shown to only slightly affect cell substrate adhesion <a href="http://www.ncbi.nlm.nih.gov/pubmed/10411959"> (Weber 1996)</a>, growth and pinocytosis <a href="http://www.ncbi.nlm.nih.gov/pubmed/10413681"> (Rivero et al. 1999)</a>, and development <a href="http://www.ncbi.nlm.nih.gov/pubmed/10704840"> (Ponte et al. 2000)</a>. A redundancy in the microfilament system was suggested when two cytoskeletal genes, <i>abpA</i> and <a href="/gene/DDB_G0269100">abpC</a>, were disrupted. The loss of both proteins severely affected growth and resistance to osmotic stress. It also resulted in reduced motility and phagocytosis rates, and heavily impaired development. These changes were reversed by expressing either <i>abpA</i> or <i>abpC</i>, showing the defects to be due to the absence of the two F-actin cross-linking proteins <a href="http://www.ncbi.nlm.nih.gov/pubmed/1732064"> (Witke et al. 1992)</a>, <a href="http://www.ncbi.nlm.nih.gov/pubmed/8937986"> (Rivero et al. 1996)</a>.<curation_status>Gene has been comprehensively annotated, 19-SEP-2003 PF</curation_status></summary>Output:
DDB_G0268632 Petra Fey ''abpA'' gene encodes alpha-actinin, a 95 kD protein originally isolated from the cell cortex. It forms a dimer, crosslinks actin filaments ([/ontology/go/0051017/annotation/page/1 actin filament bundle formation]) into lateral arrays, and increases the actin-stimulated Mg ATPase of myosin. Both activities are regulated by Ca2+ [http://www.ncbi.nlm.nih.gov/pubmed/6746725 (Condeelis et al. 1984)]. The alpha-actinin molecule carries two characteristic EF-hand structures. The calcium-binding loops form the structural basis for the calcium sensitivity ([/ontology/go/0005509/annotation/page/1 calcium ion binding]) [http://www.ncbi.nlm.nih.gov/pubmed/3622778 (Noegel et al. 1987)]. It was shown that EF hand I has a low affinity for Ca2+ and EF hand II a high affinity, implying a regulatory function of EF hand I in the inhibition of F-actin cross-linking activity [http://www.ncbi.nlm.nih.gov/pubmed/8486739 (Witke et al. 1993)]. This was confirmed when the viscoelastic properties of F-actin solutions in the presence of mutated EF hand structures was tested, and it was concluded that the first EF hand of alpha-actinin is crucial for its crosslinking function [http://www.ncbi.nlm.nih.gov/pubmed/8561496 (Janssen et al. 1996)].<br />The phenotype of an alpha-actinin mutant, HG1130, which retained only trace amounts of alpha-actinin, appeared to be normal [http://www.ncbi.nlm.nih.gov/pubmed/3956480 (Wallraff et al. 1986)]. The lack of alpha-actinin was shown to only slightly affect cell substrate adhesion [http://www.ncbi.nlm.nih.gov/pubmed/10411959 (Weber 1996)], growth and pinocytosis [http://www.ncbi.nlm.nih.gov/pubmed/10413681 (Rivero et al. 1999)], and development [http://www.ncbi.nlm.nih.gov/pubmed/10704840 (Ponte et al. 2000)]. A redundancy in the microfilament system was suggested when two cytoskeletal genes, ''abpA'' and [/gene/DDB_G0269100 abpC], were disrupted. The loss of both proteins severely affected growth and resistance to osmotic stress. It also resulted in reduced motility and phagocytosis rates, and heavily impaired development. These changes were reversed by expressing either ''abpA'' or ''abpC'', showing the defects to be due to the absence of the two F-actin cross-linking proteins [http://www.ncbi.nlm.nih.gov/pubmed/1732064 (Witke et al. 1992)], [http://www.ncbi.nlm.nih.gov/pubmed/8937986 (Rivero et al. 1996)].Gene has been comprehensively annotated, 19-SEP-2003 PF
The
Input: A summary paragraph (XML) like below
Output: MediaWiki (converted using
HTML::WikiConverter)Note: _Ignore the first two columns of Output - DDBGID & Author Name