| RRC ID |
6448
|
| Author |
Xiong G, Qadota H, Mercer KB, McGaha LA, Oberhauser AF, Benian GM.
|
| Title |
A LIM-9 (FHL)/SCPL-1 (SCP) complex interacts with the C-terminal protein kinase regions of UNC-89 (obscurin) in Caenorhabditis elegans muscle.
|
| Journal |
J Mol Biol
|
| Abstract |
The C. elegans gene unc-89 encodes a set of mostly giant polypeptides (up to 900 kDa) that contain multiple immunoglobulin (Ig) and fibronectin type 3 (Fn3), a triplet of SH3-DH-PH, and two protein kinase domains. The loss of function mutant phenotype and localization of antibodies to UNC-89 proteins indicate that the function of UNC-89 is to help organize sarcomeric A-bands, especially M-lines. Recently, we reported that each of the protein kinase domains interacts with SCPL-1, which contains a CTD-type protein phosphatase domain. Here, we report that SCPL-1 interacts with LIM-9 (FHL), a protein that we first discovered as an interactor of UNC-97 (PINCH) and UNC-96, components of an M-line costamere in nematode muscle. We show that LIM-9 can interact with UNC-89 through its first kinase domain and a portion of unique sequence lying between the two kinase domains. All the interactions were confirmed by biochemical methods. A yeast three-hybrid assay demonstrates a ternary complex between the two protein kinase regions and SCPL-1. Evidence that the UNC-89/SCPL-1 interaction occurs in vivo was provided by showing that over-expression of SCPL-1 results in disorganization of UNC-89 at M-lines. We suggest two structural models for the interactions of SCPL-1 and LIM-9 with UNC-89 at the M-line.
|
| Volume |
386(4)
|
| Pages |
976-88
|
| Published |
2009-3-6
|
| DOI |
10.1016/j.jmb.2009.01.016
|
| PII |
S0022-2836(09)00050-3
|
| PMID |
19244614
|
| PMC |
PMC4321865
|
| MeSH |
Amino Acid Sequence
Animals
Animals, Genetically Modified
Caenorhabditis elegans / enzymology*
Caenorhabditis elegans Proteins / chemistry
Caenorhabditis elegans Proteins / metabolism*
Carrier Proteins / metabolism*
LIM Domain Proteins
Models, Biological
Molecular Sequence Data
Muscle Proteins / chemistry*
Muscle Proteins / metabolism*
Muscles / cytology
Muscles / enzymology*
Phosphoprotein Phosphatases / metabolism*
Protein Binding
Protein Transport
Reproducibility of Results
Two-Hybrid System Techniques
|
| IF |
4.76
|
| Times Cited |
25
|
|
WOS Category
|
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
| Resource |
| C.elegans |
tm752 |
