A mechanistic design principle for protein tyrosine kinase sensors: application to a validated cancer target.
A new mechanistic principle for reporting the phosphorylation of tyrosine is described, which should prove applicable to even the most fastidious of protein tyrosine kinases, as demonstrated by the acquisition of a fluorescent sensor for the extraordinarily demanding anaplastic lymphoma kinase.
Wakata
Aya
A
Department of Biochemistry, The Albert Einstein College of Medicine of Yeshiva University, 1300 Morris Park Avenue, Bronx, New York 10461, USA.
Cahill
Sean M
SM
Blumenstein
Michael
M
Gunby
Rosalind H
RH
Jockusch
Steffen
S
Marti
Angel A
AA
Cimbro
Barbara
B
Gambacorti-Passerini
Carlo
C
Donella-Deana
Arianna
A
Pinna
Lorenzo A
LA
Turro
Nicholas J
NJ
Lawrence
David S
DS
D000595:Amino Acid Sequence; D000077548:Anaplastic Lymphoma Kinase; D000970:Antineoplastic Agents / Q000737:chemistry; D005456:Fluorescent Dyes; D015394:Molecular Structure; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*; D020794:Receptor Protein-Tyrosine Kinases; D014443:Tyrosine / Q000378:metabolism*
D000970:Antineoplastic Agents; D005456:Fluorescent Dyes; D014443:Tyrosine; D000077548:Anaplastic Lymphoma Kinase; D011505:Protein-Tyrosine Kinases; D020794:Receptor Protein-Tyrosine Kinases