KIBRA is a novel substrate for protein kinase Cζ

Büther, Katrin; Plaas, Christian; Barnekow, Angelika; Kremerskothen, Joachim

doi:10.1016/j.bbrc.2004.03.107

Cited by 97 publications

(103 citation statements)

References 18 publications

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“…Human KIBRA has been reported to play a role in cell migration and is known to be phosphorylated by protein kinase C (PKC) zeta. [27][28][29] MSTs and LATs members of the SWH pathway have previously been shown to be epigenetically inactivated in certain human cancers. Frequent methylation of MST2 (96%) was found in head and neck squamous cell carcinoma and less frequently for LATS1 (24%) and LATS2 (8%).…”

Section: ©2 0 1 1 L a N D E S B I O S C I E N C E D O N O T D I S Tmentioning

confidence: 99%

Frequent epigenetic inactivation ofKIBRA,an upstream member of the Salvador/Warts/Hippo (SWH) tumor suppressor network, is associated with specific genetic event in B-cell acute lymphocytic leukemia

et al. 2011

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Section: ©2 0 1 1 L a N D E S B I O S C I E N C E D O N O T D I S Tmentioning

confidence: 99%

Frequent epigenetic inactivation ofKIBRA,an upstream member of the Salvador/Warts/Hippo (SWH) tumor suppressor network, is associated with specific genetic event in B-cell acute lymphocytic leukemia

et al. 2011

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“…KIBRA (kidney and brain expressed protein; gene locus 5q34-q35.2), a scaffolding protein, is expressed in the murine and human brain, with the highest expression levels in the hippocampus and the temporal lobe (Johannsen, Duning, Pavenstadt, Kremerskothen, & Boeckers, 2008;Papassotiropoulos et al, 2006), regions known to be involved in episodic memory (Davachi, 2006;Eichenbaum, Yonelinas, & Ranganath, 2007;Rempel-Clower, Zola, Squire, & Amaral, 1996;Scoville & Milner, 1957;Squire, Wixted, & Clark, 2007;ZolaMorgan, Squire, & Amaral, 1986). KIBRA has been proposed to be involved in processes important to episodic memory formation, such as signal transduction, synaptic plasticity, long-term potentiation, and synaptic transmission (Buther, Plaas, Barnekow, & Kremerskothen, 2004;Johannsen et al, 2008;Kremerskothen et al, 2003). In the rat brain, KIBRA expression is highest during the early stages of synaptogenesis and might therefore play an important function in brain development besides its role in modifying existing synapses (Johannsen et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

KIBRA and CLSTN2 polymorphisms exert interactive effects on human episodic memory

Preuschhof

Heekeren

et al. 2010

Neuropsychologia

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a b s t r a c tIndividual differences in episodic memory are highly heritable. Several studies have linked a polymorphism in the gene encoding the KIBRA protein to episodic memory performance. Results regarding CLSTN2, the gene encoding the synaptic protein calsyntenin 2, have been less consistent, possibly pointing to interactions with other genes. Given that both KIBRA and CLSTN2 are expressed in the medial temporal lobe and have been linked to synaptic plasticity, we investigated whether KIBRA and CLSTN2 interactively modulate episodic memory performance (n = 383). We replicated the beneficial effect of the KIBRA T-allele on episodic memory, and discovered that this effect increases with the associative demands of the memory task. Importantly, the memory-enhancing effect of the KIBRA T-allele was boosted by the presence of the CLSTN2 C-allele, which positively affected memory performance in some previous studies. In contrast, the presence of CLSTN2 C-allele led to reduced performance in subjects homozygous for the KIBRA C-allele. Overall, these findings suggest that KIBRA and CLSTN2 interactively modulate episodic memory performance, and underscore the need for delineating the interactive effects of multiple genes on brain and behavior.

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“…Sequencing of the proteins in individual bands revealed the presence of a novel DLC1-interacting protein termed KIBRA. KIBRA was originally identified as a dendrin-interacting protein expressed predominantly in kidney and brain (9,10). It contains two N-terminal WW domains, an internal C2-like domain, and a C-terminal region rich in glutamic acids.…”

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confidence: 99%

Essential Role of KIBRA in Co-activator Function of Dynein Light Chain 1 in Mammalian Cells

Rayala

Hollander

Manavathi

et al. 2006

Journal of Biological Chemistry

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Recently dynein light chain 1 (DLC1), a cytoskeleton signaling component, has been shown to interact with and transactivate estrogen receptor-␣ (ER), leading to increased expression of ER target genes and growth stimulation of breast cancer cells. However, the molecular mechanism by which DLC1 regulates the ER pathway remains poorly understood. To gain insights into the putative mechanism, here we set out to identify novel DLC1-interacting proteins. We identified KIBRA, a WW domain-and a glutamic acid stretch-containing protein, as a DLC1-binding protein and showed that it interacts with DLC1 both in vitro and in vivo. We found that KIBRA-DLC1 complex is recruited to ER-responsive promoters. We also found that KIBRA-DLC1 interaction is mandatory for the recruitment and transactivation functions of ER or DLC1 to the target chromatin. Finally we found that KIBRA interacts with histone H3 via its glutamic acid-rich region and that such interaction might play a mechanistic role in conferring an optimal ER transactivation function as well as the proliferation of ligand-stimulated breast cancer cells. Together these findings indicate that DLC1-KIBRA interaction is essential for ER transactivation in breast cancer cells.Breast cancer is one of the most common malignancies among women. Despite several advances in diagnosis and therapy, breast cancer remains a significant public health problem with high morbidity and mortality. Overwhelming data from clinical and tissue culture model systems suggest that the estrogen pathway plays a crucial role in the development of female breast cancer (1, 2). Estrogen receptor ␣ (ER) 3 belongs to a superfamily of ligand-activated transcription factors whose transcriptional activities are influenced by numerous signaling pathways. ER consists of an N-terminal hormone-independent transcriptional AF1 domain, a central DNA-binding domain with two zinc fingers, and a C-terminal ligand-binding domain with a hormone-dependent transcriptional AF2 domain (3). The classic mechanism of ER activation involves ligand binding leading to the receptor dimerization and direct interaction with estrogen response elements (EREs) in the promoter regions of target genes (4, 5). ER also regulates transcription through nonclassic response sites involving other transcription factors, such as Sp1, c-Jun, and AP-1, probably via protein-protein interactions (6).Recently we identified DLC1 as an ER-interacting protein. DLC1, an 8-kDa component of the cytoplasmic dynein complex, is highly conserved among species and widely expressed in a number of tissues. In addition to playing an essential role in dynein motor function, DLC1 interacts with a number of proteins of diverse functions. DLC1 is a physiologically interactive substrate of Pak1, and their interaction is essential for the cell survival functions of both Pak1 and DLC1 (7). Furthermore DLC1 up-regulation and its phosphorylation by Pak1 promote the growth of ER-positive breast cancer cells. Conditional up-regulation of DLC1 facilitates estrogen-induced ER t...

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KIBRA is a novel substrate for protein kinase Cζ

Cited by 97 publications

References 18 publications

Frequent epigenetic inactivation ofKIBRA,an upstream member of the Salvador/Warts/Hippo (SWH) tumor suppressor network, is associated with specific genetic event in B-cell acute lymphocytic leukemia

Frequent epigenetic inactivation ofKIBRA,an upstream member of the Salvador/Warts/Hippo (SWH) tumor suppressor network, is associated with specific genetic event in B-cell acute lymphocytic leukemia

KIBRA and CLSTN2 polymorphisms exert interactive effects on human episodic memory

Essential Role of KIBRA in Co-activator Function of Dynein Light Chain 1 in Mammalian Cells

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