Spatial restriction of PDK1 activation cascades by anchoring to mAKAPα

Jennifer J. Carlisle Michel, Ian K. Townley, Kimberly L. Dodge-Kafka, Fang Zhang, Michael S Kapiloff, John D. Scott

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

The muscle A-kinase anchoring protein (mAKAP) tethers cAMP-dependent enzymes to perinuclear membranes of cardiomyocytes. We now demonstrate that two alternatively spliced forms of mAKAP are expressed: mAKAPα and mAKAPβ. The longer form, mAKAPα, is preferentially expressed in the brain. mAKAPβ is a shorter form of the anchoring protein that lacks the first 244 amino acids and is preferentially expressed in the heart. The unique amino terminus of mAKAPα can spatially restrict the activity of 3-phosphoinositide-dependent kinase-1 (PDK1). Biochemical and genetic analyses demonstrate that simultaneous recruitment of PDK1 and ERK onto mAKAPα facilitates activation and release of the downstream target p90RSK. The assembly of tissue-specific signaling complexes provides an efficient mechanism to integrate and relay lipid-mediated and mitogenic activated signals to the nucleus.

Original languageEnglish
Pages (from-to)661-672
Number of pages12
JournalMolecular Cell
Volume20
Issue number5
DOIs
StatePublished - Dec 9 2005
Externally publishedYes

Fingerprint

1-Phosphatidylinositol 4-Kinase
Protein Kinases
Muscles
Muscle Proteins
3-Phosphoinositide-Dependent Protein Kinases
Cardiac Myocytes
Molecular Biology
Lipids
Amino Acids
Membranes
Brain
Enzymes

ASJC Scopus subject areas

  • Molecular Biology

Cite this

Carlisle Michel, J. J., Townley, I. K., Dodge-Kafka, K. L., Zhang, F., Kapiloff, M. S., & Scott, J. D. (2005). Spatial restriction of PDK1 activation cascades by anchoring to mAKAPα. Molecular Cell, 20(5), 661-672. https://doi.org/10.1016/j.molcel.2005.10.013

Spatial restriction of PDK1 activation cascades by anchoring to mAKAPα. / Carlisle Michel, Jennifer J.; Townley, Ian K.; Dodge-Kafka, Kimberly L.; Zhang, Fang; Kapiloff, Michael S; Scott, John D.

In: Molecular Cell, Vol. 20, No. 5, 09.12.2005, p. 661-672.

Research output: Contribution to journalArticle

Carlisle Michel, JJ, Townley, IK, Dodge-Kafka, KL, Zhang, F, Kapiloff, MS & Scott, JD 2005, 'Spatial restriction of PDK1 activation cascades by anchoring to mAKAPα', Molecular Cell, vol. 20, no. 5, pp. 661-672. https://doi.org/10.1016/j.molcel.2005.10.013
Carlisle Michel JJ, Townley IK, Dodge-Kafka KL, Zhang F, Kapiloff MS, Scott JD. Spatial restriction of PDK1 activation cascades by anchoring to mAKAPα. Molecular Cell. 2005 Dec 9;20(5):661-672. https://doi.org/10.1016/j.molcel.2005.10.013
Carlisle Michel, Jennifer J. ; Townley, Ian K. ; Dodge-Kafka, Kimberly L. ; Zhang, Fang ; Kapiloff, Michael S ; Scott, John D. / Spatial restriction of PDK1 activation cascades by anchoring to mAKAPα. In: Molecular Cell. 2005 ; Vol. 20, No. 5. pp. 661-672.
@article{aa7dd9911fe840b4a2a50ae691ceb56b,
title = "Spatial restriction of PDK1 activation cascades by anchoring to mAKAPα",
abstract = "The muscle A-kinase anchoring protein (mAKAP) tethers cAMP-dependent enzymes to perinuclear membranes of cardiomyocytes. We now demonstrate that two alternatively spliced forms of mAKAP are expressed: mAKAPα and mAKAPβ. The longer form, mAKAPα, is preferentially expressed in the brain. mAKAPβ is a shorter form of the anchoring protein that lacks the first 244 amino acids and is preferentially expressed in the heart. The unique amino terminus of mAKAPα can spatially restrict the activity of 3-phosphoinositide-dependent kinase-1 (PDK1). Biochemical and genetic analyses demonstrate that simultaneous recruitment of PDK1 and ERK onto mAKAPα facilitates activation and release of the downstream target p90RSK. The assembly of tissue-specific signaling complexes provides an efficient mechanism to integrate and relay lipid-mediated and mitogenic activated signals to the nucleus.",
author = "{Carlisle Michel}, {Jennifer J.} and Townley, {Ian K.} and Dodge-Kafka, {Kimberly L.} and Fang Zhang and Kapiloff, {Michael S} and Scott, {John D.}",
year = "2005",
month = "12",
day = "9",
doi = "10.1016/j.molcel.2005.10.013",
language = "English",
volume = "20",
pages = "661--672",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "5",

}

TY - JOUR

T1 - Spatial restriction of PDK1 activation cascades by anchoring to mAKAPα

AU - Carlisle Michel, Jennifer J.

AU - Townley, Ian K.

AU - Dodge-Kafka, Kimberly L.

AU - Zhang, Fang

AU - Kapiloff, Michael S

AU - Scott, John D.

PY - 2005/12/9

Y1 - 2005/12/9

N2 - The muscle A-kinase anchoring protein (mAKAP) tethers cAMP-dependent enzymes to perinuclear membranes of cardiomyocytes. We now demonstrate that two alternatively spliced forms of mAKAP are expressed: mAKAPα and mAKAPβ. The longer form, mAKAPα, is preferentially expressed in the brain. mAKAPβ is a shorter form of the anchoring protein that lacks the first 244 amino acids and is preferentially expressed in the heart. The unique amino terminus of mAKAPα can spatially restrict the activity of 3-phosphoinositide-dependent kinase-1 (PDK1). Biochemical and genetic analyses demonstrate that simultaneous recruitment of PDK1 and ERK onto mAKAPα facilitates activation and release of the downstream target p90RSK. The assembly of tissue-specific signaling complexes provides an efficient mechanism to integrate and relay lipid-mediated and mitogenic activated signals to the nucleus.

AB - The muscle A-kinase anchoring protein (mAKAP) tethers cAMP-dependent enzymes to perinuclear membranes of cardiomyocytes. We now demonstrate that two alternatively spliced forms of mAKAP are expressed: mAKAPα and mAKAPβ. The longer form, mAKAPα, is preferentially expressed in the brain. mAKAPβ is a shorter form of the anchoring protein that lacks the first 244 amino acids and is preferentially expressed in the heart. The unique amino terminus of mAKAPα can spatially restrict the activity of 3-phosphoinositide-dependent kinase-1 (PDK1). Biochemical and genetic analyses demonstrate that simultaneous recruitment of PDK1 and ERK onto mAKAPα facilitates activation and release of the downstream target p90RSK. The assembly of tissue-specific signaling complexes provides an efficient mechanism to integrate and relay lipid-mediated and mitogenic activated signals to the nucleus.

UR - http://www.scopus.com/inward/record.url?scp=28444443387&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=28444443387&partnerID=8YFLogxK

U2 - 10.1016/j.molcel.2005.10.013

DO - 10.1016/j.molcel.2005.10.013

M3 - Article

C2 - 16337591

AN - SCOPUS:28444443387

VL - 20

SP - 661

EP - 672

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 5

ER -