Abstract
PTB domains are protein modules that usually interact with the cytoplasmic tail of a wide variety of growth factor receptors. In so doing, they mediate the transduction of extracellular information to specific downstream targets within the cell that ultimately determine the fate of a number of important biological processes such as cell growth and differentiation, cell cycle regulation and apoptosis. Recent structural and functional studies of PTB domains from a variety of cellular proteins have begun to shed light on the molecular mechanisms of action of these important protein modules. In the present review, we provide an account of such studies and suggest that PTB domains can be subdivided into three distinct categories on the basis of their topological differences. We also discuss the various mechanisms employed by the PTB domains in recognition of a diverse set of ligands without a consensus sequence. Finally, we discuss the role of molecular plasticity as a possible determinant of functional versatility of PTB domains.
| Original language | English |
|---|---|
| Pages (from-to) | 547-556 |
| Number of pages | 10 |
| Journal | IUBMB Life |
| Volume | 56 |
| Issue number | 9 |
| DOIs | |
| State | Published - Sep 1 2004 |
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Keywords
- Cancer
- Conformational change
- Growth factor receptors
- Ligand binding
- Promiscuity
- PTB sub-family
- Signal transduction
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
Cite this
PTB or not to be : Promiscuous, tolerant and bizarro domains come of age. / Farooq, Amjad; Zhou, Ming Ming.
In: IUBMB Life, Vol. 56, No. 9, 01.09.2004, p. 547-556.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - PTB or not to be
T2 - Promiscuous, tolerant and bizarro domains come of age
AU - Farooq, Amjad
AU - Zhou, Ming Ming
PY - 2004/9/1
Y1 - 2004/9/1
N2 - PTB domains are protein modules that usually interact with the cytoplasmic tail of a wide variety of growth factor receptors. In so doing, they mediate the transduction of extracellular information to specific downstream targets within the cell that ultimately determine the fate of a number of important biological processes such as cell growth and differentiation, cell cycle regulation and apoptosis. Recent structural and functional studies of PTB domains from a variety of cellular proteins have begun to shed light on the molecular mechanisms of action of these important protein modules. In the present review, we provide an account of such studies and suggest that PTB domains can be subdivided into three distinct categories on the basis of their topological differences. We also discuss the various mechanisms employed by the PTB domains in recognition of a diverse set of ligands without a consensus sequence. Finally, we discuss the role of molecular plasticity as a possible determinant of functional versatility of PTB domains.
AB - PTB domains are protein modules that usually interact with the cytoplasmic tail of a wide variety of growth factor receptors. In so doing, they mediate the transduction of extracellular information to specific downstream targets within the cell that ultimately determine the fate of a number of important biological processes such as cell growth and differentiation, cell cycle regulation and apoptosis. Recent structural and functional studies of PTB domains from a variety of cellular proteins have begun to shed light on the molecular mechanisms of action of these important protein modules. In the present review, we provide an account of such studies and suggest that PTB domains can be subdivided into three distinct categories on the basis of their topological differences. We also discuss the various mechanisms employed by the PTB domains in recognition of a diverse set of ligands without a consensus sequence. Finally, we discuss the role of molecular plasticity as a possible determinant of functional versatility of PTB domains.
KW - Cancer
KW - Conformational change
KW - Growth factor receptors
KW - Ligand binding
KW - Promiscuity
KW - PTB sub-family
KW - Signal transduction
UR - http://www.scopus.com/inward/record.url?scp=10344234238&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=10344234238&partnerID=8YFLogxK
U2 - 10.1080/15216540400013895
DO - 10.1080/15216540400013895
M3 - Article
VL - 56
SP - 547
EP - 556
JO - IUBMB Life
JF - IUBMB Life
SN - 1521-6543
IS - 9
ER -