The PH domain: a common piece in the structural pathcwork of signalling proteins

Musacchio, Andrea; Gibson, Toby J.; Rice, Peter; Thompson, Julie; Saraste, Matti

doi:10.1016/0968-0004(93)90071-t

Cited by 530 publications

(385 citation statements)

References 35 publications

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“…Catalytic domains are boxed. PBD stands for p21 binding domain and PH stands for pleckstrin homology domain (Musacchio et al, 1993). Percent similarities were calculated based on alignments by DNASTAR cally-labelled NIH3T3 cells ( Figure 3b).…”

Section: Resultsmentioning

confidence: 99%

A novel human SPS1/STE20 homologue, KHS, activates Jun N-terminal kinase

Tung

Blenis

1997

Oncogene

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STE20-homologous proteins have been implicated in mammalian MAP kinase pathways as important transducers of signals from p21 family GTPases. We have cloned a novel STE20 family member, which we call KHS for kinase homologous to SPS1/STE20, that encodes a kinase of 95 kD which is expressed in a variety of tissues. Transiently expressed fusion protein GST-KHS exhibits phosphotransferase activity toward a panel of test substrates, including myelin basic protein (MBP), which is phosphorylated by all known STE20 homologues. KHS is most closely related to another human STE20, GC kinase (74% similar in the catalytic domain), which has recently been placed upstream of the stress-activated MAP kinases (SAPKs/JNKs. KHS also activates JNK in transient coexpression experiments, suggesting a role for KHS in the stress response of ®broblasts. Characterization and comparison of the regulation of these two kinases will be important in elucidating MAP kinase signalling cascades.

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Section: Resultsmentioning

confidence: 99%

A novel human SPS1/STE20 homologue, KHS, activates Jun N-terminal kinase

Tung

Blenis

1997

Oncogene

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“…A protein serine/threonine kinase domain was present in the amino-terminal region (amino acids 76-338) [12], and a coiled-coil forming region predicted by the algorithm of Lupas et al [15] (amino acids 460-1068) followed. A pleckstrin homology domain [16] and a cysteine-rich zinc finger motif [17] exist in the carboxyl-terminal region (Fig. 1B).…”

Section: Cdna Cloning and Characterization Of Mouse Pl60mentioning

confidence: 99%

ROCK‐I and ROCK‐II, two isoforms of Rho‐associated coiled‐coil forming protein serine/threonine kinase in mice

et al. 1996

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We recently identified a novel human protein kinase, p160 ROCK, as a putative downstream target of the small GTPase Rho. Using the human ROCK cDNA as a probe, we isolated cDNA of two distinct, highly related sequences from mouse libraries. One encoded a mouse counterpart of human ROCK (ROCK-I), and the other encoded a novel ROCK-related kinase (ROCK-II). Like ROCK/ROCK-I, ROCK-II also bound to GTP-Rho selectively. ROCK-I mRNA was ubiquitously expressed except in the brain and muscle, whereas ROCK-II mRNA was expressed abundantly in the brain, muscle, heart, lung and placenta. These results suggest that at least two ROCK isoforms are present in a single species and play distinct roles in Rho-mediated signalling pathways.

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“…by dashes and a 83 aa insertion in p160 R°cK is indicated. Homologies between these three proteins are boxed, related residues being grouped as follows: EDQN; RKH; LVI; FYW; ST; GA. A consensus sequence for PH domains [23] is shown below; residues from this sequence conserved in at least 50% of the 71 reported PH domains [23,26] are marked by stars. The six PH sub-domains are indicated.…”

Section: Rho and Racl Interact Directly With Citron In Vitromentioning

confidence: 99%

“…1130. Comparison with a consensus sequence for PH don,,ains [23] revealed 33% identities over 51 aa (PH sub-domains 1 II, I/I, and VI). A single reported PH region (oxysterol binding protein, aa 89-180, Genbank accession M86917) s,:ored better, displaying a block of 8 aa entirely conserved in c~tron.…”

Section: The Predicted Sequence Of Citron Contains Signalmentioning

confidence: 99%

A novel partner for the GTP‐bound forms of rho and rac

et al. 1995

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Ahstract Using the yeast two hybrid system and overlay assays we identified a putative rholrac effector, citron, which interacts with the GTP-bound forms of rho and racl, but not with cdc42. Extensive homologies to known proteins were not observed. This 183 kDa protein contains a C~H2 zinc finger, a PH domain, and a long coiled-coil forming region including 4 leucine zippers and the rholrac binding site. We recently identified three others putative rho effeetors characterized by a common rho binding motif. Citron does not share this motif and displays a distinctive protein organization, thus defining a separate class of rho partners.

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The PH domain: a common piece in the structural pathcwork of signalling proteins

Cited by 530 publications

References 35 publications

A novel human SPS1/STE20 homologue, KHS, activates Jun N-terminal kinase

A novel human SPS1/STE20 homologue, KHS, activates Jun N-terminal kinase

ROCK‐I and ROCK‐II, two isoforms of Rho‐associated coiled‐coil forming protein serine/threonine kinase in mice

A novel partner for the GTP‐bound forms of rho and rac

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