The Caenorhabditis elegans p21-activated Kinase (CePAK) Colocalizes with CeRac1 and CDC42Ce at Hypodermal Cell Boundaries during Embryo Elongation

Chen, Wei-Ning; Chen, Shan; Yap, Seow Fong; Lim, Louis

doi:10.1074/jbc.271.42.26362

Cited by 54 publications

(41 citation statements)

References 32 publications

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“…Caenorhabditis elegans pak-1 has previously been cloned by degenerate PCR and has been shown to co-localize with CED-10 and CDC-42 at late embryonic stages (Chen et al, 1996). Few data exist on the other PAK (C45B11.1), which we find is SL1 transspliced and will be hereafter referred to as C. elegans pak-2.…”

Section: Max-2 Is Required For Commissural Axon Guidance Of the Vccmnmentioning

confidence: 57%

The Caenorhabditis elegans P21-activated kinases are differentially required for UNC-6/netrin-mediated commissural motor axon guidance

et al. 2006

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P21 activated kinases (PAKs) are major downstream effectors of rac-related small GTPases that regulate various cellular processes. We have identified the new PAK gene max-2 in a screen for mutants disrupted in UNC-6/netrin-mediated commissural axon guidance. There are three Caenorhabditis elegans PAKs. We find that each C. elegansPAK represents a distinct group previously identified in other species. Here we examine their roles in the postembryonic migration of the P cell neuroblasts and the axon guidance of the ventral cord commissural motoneurons(VCCMNs). We find that the two PAKs, max-2 and pak-1, are redundantly required for P cell migration and function with UNC-73/Trio and the rac GTPases (CED-10 and MIG-2). During axon guidance of the VCCMNs, PAK-1 also acts with the rac GTPases, CED-10 and MIG-2, and is completely redundant with MAX-2. Interestingly, we find that unlike MAX-2 activity during P cell migration, for motoneuron axon guidance max-2 is also required in parallel to this PAK-1 pathway, independent of rac GTPase signaling. Finally,we provide evidence that MAX-2 functions downstream of the UNC-6/netrin receptor UNC-5 during axon repulsion and is an integral part of its signaling.

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Section: Max-2 Is Required For Commissural Axon Guidance Of the Vccmnmentioning

confidence: 57%

The Caenorhabditis elegans P21-activated kinases are differentially required for UNC-6/netrin-mediated commissural motor axon guidance

et al. 2006

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“…Taking the evolutional distance between mammals and nematodes into consideration, conservation in the kinase domains of ULKs and UNC-51 (60 ± 65% amino acid identity) is comparable to those in the other well characterized kinase subfamilies. For example, kinase domains of nematode and mammalian PKA (Gross et al, 1990), PKCb (Land et al, 1994), PKCd, (Tabuse et al, 1989), PAK (Chen et al, 1996) and PKB (Paradis and Ruvkun, 1998), have 80%, 76%, 64%, 49%, and 35%, amino acid identity, respectively. Apart from the similarity within the kinase domain, ULKs and UNC-51 retain evolutionary conserved domain structures consisting of the kinase, PS and C domains.…”

Section: Discussionmentioning

confidence: 99%

Mouse ULK2, a novel member of the UNC-51-like protein kinases: unique features of functional domains

Yan¹,

et al. 1999

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The UNC-51 serine/threonine kinase of C. elegans plays an essential role in axonal elongation, and unc-51 mutants exhibit uncoordinated movements. We have previously identi®ed mouse and human cDNAs encoding UNC-51-like kinase (ULK1). Here we report the identi®cation and characterization of the second murine member of this kinase family, ULK2. Mouse ULK2 cDNA encodes a putative polypeptide of 1033 aa which has an overall 52% and 33% amino acid identity to ULK1 and UNC-51, respectively. ULKs and UNC-51 share a typical domain structure of an amino-terminal kinase domain, a central proline/serine rich (PS) domain, and a carboxy-terminal (C) domain. Northern blot analysis showed that ULK2 mRNA is widely expressed in adult tissues. In situ hybridization analysis indicated that ULK2 mRNA is ubiquitously localized in premature as well as mature neurons in developing nervous system. ULK2 gene was mapped to mouse chromosome 11B1.3 and rat chromosome 10q23 by FISH. HA-tagged ULK2 expressed in COS7 cells had an apparent molecular size of *150 kDa and was autophosphorylated in vitro. Truncation mutants suggested that the autophosphorylation occurs in the PS domain. Although expression of ULK2 failed to rescue unc-51 mutant of C. elegans, a series of ULK2/UNC-51 chimeric kinases revealed that function of the kinase and PS domains are conserved among species, while the C domain acts in a speciesspeci®c manner. These results suggest that ULK2 is involved in a previously uncharacterized signaling pathway in mammalian cells.

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“…42) and Rac-1 (CED-10) localize to epidermal cell borders (Chen et al, 1996), and Rho-family GTPases appear to regulate actomyosin contractility during elongation (Wissmann et al, 1997;Wissmann et al, 1999). Beyond this, the role of Rhofamily GTPases in CeAJs is not understood.…”

Section: Adherens Junctional Domainmentioning

confidence: 99%

Sticky worms: adhesion complexes inC. elegans

Cox

Hardin

2004

Journal of Cell Science

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Caenorhabditis elegans is a powerful model system for investigating the establishment, regulation and function of adhesive structures in vivo. C. elegans has several adhesion complexes related to those in vertebrates. These include: (1) epithelial apical junctions, which have features of both adherens and tight junctions; (2) dense bodies, which are muscle-attachment structures similar to focal adhesions; (3) fibrous organelles, which resemble hemidesmosomes and mediate mechanical coupling between tissues; and (4) a putative dystrophin-glycoprotein complex that has potential roles in muscle function and embryogenesis. Recent work has increased our understanding of these structures and has given new insights into the functions of their vertebrate counterparts.

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The Caenorhabditis elegans p21-activated Kinase (CePAK) Colocalizes with CeRac1 and CDC42Ce at Hypodermal Cell Boundaries during Embryo Elongation

Cited by 54 publications

References 32 publications

The Caenorhabditis elegans P21-activated kinases are differentially required for UNC-6/netrin-mediated commissural motor axon guidance

The Caenorhabditis elegans P21-activated kinases are differentially required for UNC-6/netrin-mediated commissural motor axon guidance

Mouse ULK2, a novel member of the UNC-51-like protein kinases: unique features of functional domains

Sticky worms: adhesion complexes inC. elegans

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