| First Author | Lefebvre DC | Year | 2003 |
| Journal | Biochim Biophys Acta | Volume | 1650 |
| Issue | 1-2 | Pages | 40-9 |
| PubMed ID | 12922168 | Mgi Jnum | J:85038 |
| Mgi Id | MGI:2671550 | Doi | 10.1016/s1570-9639(03)00190-0 |
| Citation | Lefebvre DC, et al. (2003) The noncatalytic domains of Lck regulate its dephosphorylation by CD45. Biochim Biophys Acta 1650(1-2):40-9 |
| abstractText | The Src-family tyrosine kinase, Lck, contains two key regulatory phosphotyrosine residues, tyrosine 394 (Tyr-394) and tyrosine 505 (Tyr-505), both of which can be dephosphorylated by CD45. Here, the interaction of CD45 with its substrate, Lck, was determined to be complex, involving multiple interactions with both the catalytic and noncatalytic regions of Lck. CD45 preferentially dephosphorylated Tyr-394 over Tyr-505 in Lck. This was not due to sequence specificity surrounding the phosphotyrosine, but was due to the noncatalytic domains of Lck. The interactions with the noncatalytic domains of Lck and CD45 enhanced the dephosphorylation of Tyr-394 whereas intramolecular interactions within Lck reduced, but did not abolish, the dephosphorylation of Tyr-505. This demonstrates that the noncatalytic domains of Lck regulate the dephosphorylation of both Tyr-394 and Tyr-505 by CD45. |
