Molecular Cloning of a New Member of the p21-Cdc42/Rac-activated Kinase (PAK) Family

Manser, Edward; Chong, Claire; Zhao, Zhuoshen; Leung, Thomas; Michael, Gregory; Hall, Christine; Lim, Louis

doi:10.1074/jbc.270.42.25070

Cited by 232 publications

(212 citation statements)

References 33 publications

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“…1, 10, and 22), although there may be also some important differences. For example, PAK3 is released from Rac1 following activation, whereas PAK1 and PAK2 remain bound to this GTPase (2,3,6). Our analysis was performed mostly with PAK3, but we also showed that paxillin ␣ can associate with PAK1.…”

Section: Association Of Paks With Paxillin But Not Other Focal Adhesmentioning

confidence: 70%

Interaction of Paxillin with p21-activated Kinase (PAK)

Hashimoto

Tsubouchi

Mazaki

et al. 2001

Journal of Biological Chemistry

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p21-activated kinases (PAKs) are implicated in integrin signalings, and have been proposed to associate with paxillin indirectly. We show here that paxillin can bind directly to PAK3. We examined several representative focal adhesion proteins, and found that paxillin is the sole protein that associates with PAK3. PAK3 associated with the ␣ and ␤ isoforms of paxillin, but not with ␥. We also show that paxillin ␣ associated with both the kinase-inactive and the Cdc42-activated forms of PAK3 in vivo, without affecting the activation states of the kinase. A number of different functions have been ascribed to PAKs; and PAKs can bind directly to growth factor signaling-adaptor molecule, Nck, and a guanine nucleotide exchanger, ␤PIX. Our results revealed that paxillin ␣ can compete with Nck and ␤PIX in the binding of PAK3. Moreover, paxillin ␣ can be phosphorylated by PAK3 at serine. Therefore, paxillin ␣, but not ␥, appears to be capable of linking both the kinase-inactive and activated forms of PAK3 to integrins independent of Nck and ␤PIX, as Nck links PAK1 to growth factor receptors. Our results also revealed that paxillin is involved in highly complexed protein-protein interactions in integrin signaling.

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Section: Association Of Paks With Paxillin But Not Other Focal Adhesmentioning

confidence: 70%

Interaction of Paxillin with p21-activated Kinase (PAK)

Hashimoto

Tsubouchi

Mazaki

et al. 2001

Journal of Biological Chemistry

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“…The brain-specific isoform MST3b may play a distinct functional role from MST3. It has been reported that the expression pattern of a few members of STE20 kinase family is relatively restricted to a certain tissue: PAK3 in brain (49,50), hematopoietic progenitor kinase 1 in hematopoietic cells (13,14), and lymphocyte-oriented kinase in lymphocytes (23). This expression pattern may give some clues as to its possible function and physiological roles.…”

Section: Discussionmentioning

confidence: 99%

Identification of a Human Brain-specific Isoform of Mammalian STE20-like Kinase 3 That Is Regulated by cAMP-dependent Protein Kinase

Zhou¹,

Ling²,

Guo³

et al. 2000

Journal of Biological Chemistry

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“…For Cdc42, a number of molecules including Ste20/PAK serine/threonine kinases [8][9][10][11], ACK tyrosine kinase [12], phosphatidylinositol-3-ki-*Corresponding author. Fax: (81) (45) 924-5822.…”

Section: Introductionmentioning

confidence: 99%

Tyrosine phosphorylation of ACK in response to temperature shift‐down, hyperosmotic shock, and epidermal growth factor stimulation

et al. 1996

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The mammalian Cdc42 protein regulates various kinds of cellular responses, including formation of filopodia, polarization of T cells, and cell cycle progression. A non-receptor tyrosine kinase ACK, which specifically binds to the GTP-bound form of Cdc42, was isolated as a putative target of Cdc42. Here we show the induction of tyrosine phosphorylation of ACK in response to temperature shift-down to 25°C, and hypertonic shock, as well as stimulation with epidermal growth factor (EGF) in human embryonic kidney (HEK) 293 cells. The increased tyrosine phosphorylation level upon temperature shift-down was sustained for at least 60 rain, whereas reversion of the temperature to 37°C caused rapid tyrosine dephosphorylation to the initial level. The responses to EGF and the high osmolarity were transient. Furthermore, we observed association of ACK with an adaptor protein Grb2, which may suggest the involvement of Grb2 in EGF receptor-mediated tyrosine phosphorylation of ACK.

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Molecular Cloning of a New Member of the p21-Cdc42/Rac-activated Kinase (PAK) Family

Cited by 232 publications

References 33 publications

Interaction of Paxillin with p21-activated Kinase (PAK)

Interaction of Paxillin with p21-activated Kinase (PAK)

Identification of a Human Brain-specific Isoform of Mammalian STE20-like Kinase 3 That Is Regulated by cAMP-dependent Protein Kinase

Tyrosine phosphorylation of ACK in response to temperature shift‐down, hyperosmotic shock, and epidermal growth factor stimulation

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