Abstract
Tyrosine phosphorylation is usually associated with cytoplasmic events. Yet, over the years, many reports have accumulated on tyrosine phosphorylation of individual molecules in the nucleus, and several tyrosine kinases and phosphatases have been found to be at least partially nuclear. The question arises as to whether nuclear tyrosine phosphorylation represents a collection of loose ends of events originating in the cytoplasm or if there may be intranuclear signaling circuits relying on tyrosine phosphorylation to regulate specific processes. The recent discovery of a mechanism causing nuclear tyrosine phosphorylation has prompted us to review the cumulative evidence for nuclear tyrosine phosphorylation pathways and their possible role. While we found that no complex nuclear function has yet been shown to rely upon intranuclear tyrosine phosphorylation in an unambiguous fashion, we found a very high number of compelling observations on individual molecules that suggest underlying networks linking individual events. A systematic proteomics approach to nuclear tyrosine phosphorylation should help chart possible interaction pathways. (C) 2000 Elsevier Science Inc.
| Original language | English |
|---|---|
| Pages (from-to) | 1203-1215 |
| Number of pages | 13 |
| Journal | Biochemical Pharmacology |
| Volume | 60 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - Oct 15 2000 |
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Keywords
- Kinases
- Nucleus
- Proteomics
- Signal transduction
- Tyrosine phosphorylation
ASJC Scopus subject areas
- Pharmacology
Cite this
Nuclear tyrosine phosphorylation : The beginning of a map. / Cans, Christophe; Mangano, Raffaella; Barilá, Daniela; Neubauer, Gitte; Superti-Furga, Giulio.
In: Biochemical Pharmacology, Vol. 60, No. 8, 15.10.2000, p. 1203-1215.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Nuclear tyrosine phosphorylation
T2 - The beginning of a map
AU - Cans, Christophe
AU - Mangano, Raffaella
AU - Barilá, Daniela
AU - Neubauer, Gitte
AU - Superti-Furga, Giulio
PY - 2000/10/15
Y1 - 2000/10/15
N2 - Tyrosine phosphorylation is usually associated with cytoplasmic events. Yet, over the years, many reports have accumulated on tyrosine phosphorylation of individual molecules in the nucleus, and several tyrosine kinases and phosphatases have been found to be at least partially nuclear. The question arises as to whether nuclear tyrosine phosphorylation represents a collection of loose ends of events originating in the cytoplasm or if there may be intranuclear signaling circuits relying on tyrosine phosphorylation to regulate specific processes. The recent discovery of a mechanism causing nuclear tyrosine phosphorylation has prompted us to review the cumulative evidence for nuclear tyrosine phosphorylation pathways and their possible role. While we found that no complex nuclear function has yet been shown to rely upon intranuclear tyrosine phosphorylation in an unambiguous fashion, we found a very high number of compelling observations on individual molecules that suggest underlying networks linking individual events. A systematic proteomics approach to nuclear tyrosine phosphorylation should help chart possible interaction pathways. (C) 2000 Elsevier Science Inc.
AB - Tyrosine phosphorylation is usually associated with cytoplasmic events. Yet, over the years, many reports have accumulated on tyrosine phosphorylation of individual molecules in the nucleus, and several tyrosine kinases and phosphatases have been found to be at least partially nuclear. The question arises as to whether nuclear tyrosine phosphorylation represents a collection of loose ends of events originating in the cytoplasm or if there may be intranuclear signaling circuits relying on tyrosine phosphorylation to regulate specific processes. The recent discovery of a mechanism causing nuclear tyrosine phosphorylation has prompted us to review the cumulative evidence for nuclear tyrosine phosphorylation pathways and their possible role. While we found that no complex nuclear function has yet been shown to rely upon intranuclear tyrosine phosphorylation in an unambiguous fashion, we found a very high number of compelling observations on individual molecules that suggest underlying networks linking individual events. A systematic proteomics approach to nuclear tyrosine phosphorylation should help chart possible interaction pathways. (C) 2000 Elsevier Science Inc.
KW - Kinases
KW - Nucleus
KW - Proteomics
KW - Signal transduction
KW - Tyrosine phosphorylation
UR - http://www.scopus.com/inward/record.url?scp=0034668142&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034668142&partnerID=8YFLogxK
U2 - 10.1016/S0006-2952(00)00434-2
DO - 10.1016/S0006-2952(00)00434-2
M3 - Article
C2 - 11007959
AN - SCOPUS:0034668142
VL - 60
SP - 1203
EP - 1215
JO - Biochemical Pharmacology
JF - Biochemical Pharmacology
SN - 0006-2952
IS - 8
ER -