In earlier work we established that phosphoinositide 4-kinase (PI 4-kinase) may associate with transmembrane 4 superfamily (TM4SF, tetraspanin) proteins, but critical specificity issues were not addressed. Here we demonstrate that at least five different TM4SF proteins (CD9, CD63, CD81, CD151 and A15/TALLA1) can associate with a similar or identical 55kDa type II PI 4-kinase. These associations were specific, since we found no evidence for other phosphoinositide kinases (e.g. phosphoinositide 3-kinase and phosphoinositide-4-phosphate 5-kinase) associating with TM4SF proteins, and many other TM4SF proteins (including CD82 and CD53) did not associate with PI 4-kinase. CD63–PI 4-kinase complexes were almost entirely intracellular, and thus are distinct from other TM4SF–PI 4-kinase complexes (e.g. involving CD9), which are largely located in the plasma membrane. These results suggest that a specific subset of TM4SF proteins may recruit PI 4-kinase to specific membrane locations, and thereby influence phosphoinositide-dependent signalling.
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November 2000
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Research Article|
October 24 2000
Specific interactions among transmembrane 4 superfamily (TM4SF) proteins and phosphoinositide 4-kinase
Robert L. YAUCH;
Robert L. YAUCH
1
1Dana-Farber Cancer Institute, Rm D-1430, 44 Binney Street, Boston, MA 02115, U.S.A.
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Martin E. HEMLER
Martin E. HEMLER
2
1Dana-Farber Cancer Institute, Rm D-1430, 44 Binney Street, Boston, MA 02115, U.S.A.
2To whom correspondence should be addressed (e-mail martin_hemler@dfcl.harvard.edu).
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Publisher: Portland Press Ltd
Received:
February 14 2000
Revision Received:
July 07 2000
Accepted:
August 10 2000
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London © 2000
2000
Biochem J (2000) 351 (3): 629–637.
Article history
Received:
February 14 2000
Revision Received:
July 07 2000
Accepted:
August 10 2000
Citation
Robert L. YAUCH, Martin E. HEMLER; Specific interactions among transmembrane 4 superfamily (TM4SF) proteins and phosphoinositide 4-kinase. Biochem J 1 November 2000; 351 (3): 629–637. doi: https://doi.org/10.1042/bj3510629
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