Fission yeast Mor2/Cps12, a protein similar to Drosophila Furry, is essential for cell morphogenesis and its mutation induces Wee1-dependent G2 delay

Hirata, Dai; Kishimoto, Norihito; Suda, Masako; Sogabe, Yuki; Nakagawa, Sayuri; Yoshida, Yasuko; Sakai, Keisuke; Mizunuma, Masaki; Miyakawa, Tokichi; Ishiguro, Junpei; Toda, Takashi

doi:10.1093/emboj/cdf495

Cited by 62 publications

(76 citation statements)

References 71 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Its main components are two protein kinase modules, the protein kinase Nak1p (Huang et al, 2003;Leonhard and Nurse, 2005) and its regulators Sog2p (also known as Lrp1p) (Gupta et al, 2013;Kume et al, 2013) and Pmo25p (Kanai et al, 2005;Kume et al, 2007;Mendoza et al, 2005), which act upstream of the kinase Orb6p (Verde et al, 1998) and its regulator Mob2p (Hou et al, 2003). MOR signalling also requires the scaffold protein Mor2p (Hirata et al, 2002). Pmo25p, Nak1p and Sog2p localise to the SPB and the division site, whereas Mob2p, Orb6p and Mor2p only localise to the cell periphery and the division site.…”

Section: Targets Of Sid2p In the Car Checkpointmentioning

confidence: 99%

Pombe's thirteen – control of fission yeast cell division by the septation initiation network

Simanis

2015

Journal of Cell Science

View full text Add to dashboard Cite

The septation initiation network (SIN) regulates aspects of cell growth and division in Schizosaccharomyces pombe and is essential for cytokinesis. Insufficient signalling results in improper assembly of the contractile ring and failure of cytokinesis, generating multinucleated cells, whereas too much SIN signalling uncouples cytokinesis from the rest of the cell cycle. SIN signalling is therefore tightly controlled to coordinate cytokinesis with chromosome segregation. Signalling originates from the cytoplasmic face of the spindle pole body (SPB), and asymmetric localisation of some SIN proteins to one of the two SPBs during mitosis is important for regulation of the SIN. Recent studies have identified in vivo substrates of the SIN, which include components involved in mitotic control, those of the contractile ring and elements of the signalling pathway regulating polarised growth. The SIN is also required for spore formation following meiosis. This has provided insights into how the SIN performs its diverse functions in the cell cycle and shed new light on its regulation.

show abstract

Section: Targets Of Sid2p In the Car Checkpointmentioning

confidence: 99%

Pombe's thirteen – control of fission yeast cell division by the septation initiation network

Simanis

2015

Journal of Cell Science

View full text Add to dashboard Cite

show abstract

“…In addition, the subcellular localization/accumulation of Trc and Fry is interdependent in pupal wing cells (He et al, 2005). The subcellular localization of Cbk1 and Tao3 in S. cerevisiae and Orb6 and Mor2 in S. pombe (Du and Novick, 2002;Hirata et al, 2002;Nelson et al, 2003) has also been found to be interdependent, although the relationships differ in these systems (Tao3 and Mor2 are the Fry homologues in these systems).…”

Section: Introductionmentioning

confidence: 99%

DrosophilaMob Family Proteins Interact with the Related Tricornered (Trc) and Warts (Wts) Kinases

Emoto

Fang

et al. 2005

MBoC

127

View full text Add to dashboard Cite

The function of Tricornered (Trc), the Drosophila Ndr (Nuclear Dbf2-related) serine/threonine protein kinase, is required for the normal morphogenesis of a variety of polarized outgrowths including epidermal hairs, bristles, arista laterals, and dendrites. In yeast the Trc homolog Cbk1 needs to bind Mob2 to activate the RAM pathway. In this report, we provide genetic and biochemical data that Drosophila Trc also interacts with and is activated by Drosophila Dmob proteins. In addition, Drosophila Mob proteins appear to interact with the related Warts/Lats kinase, which functions as a tumor suppressor in flies and mammals. Interestingly, the overgrowth tumor phenotype that results from mutations in Dmob1 (mats) was only seen in genetic mosaics and not when the entire animal was mutant. We conclude that unlike in yeast, in Drosophila individual Mob proteins interact with multiple kinases and that individual NDR family kinases interact with multiple Mob proteins. We further provide evidence that Mo25, the Drosophila homolog of the RAM pathway hym1 gene does not function along with Trc.

show abstract

“…Furthermore, Tao3/Pag1 and Cbk1 interact physically and their localization is interdependent (23). In S. pombe, the FURRY-like protein, Mor2/Cps12, interacts physically with Orb6, the S. pombe NDR orthologue (24). The FURRY-like proteins are conserved in mammals, and thus, it is likely that other proteins interacting genetically and/or physically with S. cerevisiae Cbk1 or Dbf2 also play a role in the NDR kinase family pathway in higher eukaryotes.…”

mentioning

confidence: 99%

Mechanism of Activation of NDR (Nuclear Dbf2-related) Protein Kinase by the hMOB1 Protein

Bichsel

Tamaskovic²,

Stegert³

et al. 2004

Journal of Biological Chemistry

127

182

View full text Add to dashboard Cite

NDR (nuclear Dbf2-related) kinase belongs to a family of kinases that is highly conserved throughout the eukaryotic world. We showed previously that NDR is regulated by phosphorylation and by the Ca 2؉ -binding protein, S100B. The budding yeast relatives of Homo sapiens NDR, Cbk1, and Dbf2, were shown to interact with Mob2 (Mps one binder 2) and Mob1, respectively. This interaction is required for the activity and biological function of these kinases. In this study, we show that hMOB1, the closest relative of yeast Mob1 and Mob2, stimulates NDR kinase activity and interacts with NDR both in vivo and in vitro. The point mutations of highly conserved residues within the N-terminal domain of NDR reduced NDR kinase activity as well as human MOB1 binding. A novel feature of NDR kinases is an insert within the catalytic domain between subdomains VII and VIII. The amino acid sequence within this insert shows a high basic amino acid content in all of the kinases of the NDR family known to interact with MOB proteins. We show that this sequence is autoinhibitory, and our data indicate that the binding of human MOB1 to the N-terminal domain of NDR induces the release of this autoinhibition.NDR 1 kinase belongs to a highly conserved family of kinases, a subclass of the AGC family of protein kinases (1, 2). The NDR family consists of the mammalian protein kinases NDR1 and NDR2, Drosophila melanogaster NDR, Caenorhabditis elegans SAX1, mammalian, D. melanogaster and C. elegans large tumor suppressor kinases, Neurospora crassa COT1, Ustilago maydis UKC1, Saccharomyces cerevisiae Cbk1, Dbf2, and Dbf20, Schizosaccharomyces pombe Orb6 and Sid2, and several plant kinases (1, 2). These kinases share a high sequence conservation, and some possess conserved functions, mainly involving regulation of cell morphology and the cell cycle (2-15).The kinase domain sequence of NDR is related to that of other members of the AGC group of kinases, e.g. protein kinases A, B, C, and G, PRK, p70 S6K , p90 RSK , and phosphoinositide-dependent kinase 1 (1). NDR contains all 12 subdomains of the kinase catalytic domain as described by Hanks and Hunter (16). However, the catalytic domains of all of the members of the NDR family are interrupted by an insert of 30 -60 amino acids between subdomains VII and VIII. This inserted sequence is not well conserved but is always rich in the basic amino acids, arginine and lysine. The catalytic domain insert has been shown to act as a non-consensus nuclear localization signal in the case of NDR1. NDR1 localizes predominantly to the nucleus in COS-1 cells, whereas mutant NDR1 with a deletion in the insert is localized to the cytosol (17). An additional special feature of the NDR family of kinases is a highly conserved N-terminal domain. In the case of NDR1, this domain consists of 81 amino acids and encompasses a region predicted to form an amphiphilic ␣-helix that binds to the EF-hand Ca 2ϩ -binding protein, S100B (18). Finally, the Cterminal extension of NDR kinase contains a broadly conserved hydrophobic motif ...

show abstract

Fission yeast Mor2/Cps12, a protein similar to Drosophila Furry, is essential for cell morphogenesis and its mutation induces Wee1-dependent G2 delay

Cited by 62 publications

References 71 publications

Pombe's thirteen – control of fission yeast cell division by the septation initiation network

Pombe's thirteen – control of fission yeast cell division by the septation initiation network

DrosophilaMob Family Proteins Interact with the Related Tricornered (Trc) and Warts (Wts) Kinases

Mechanism of Activation of NDR (Nuclear Dbf2-related) Protein Kinase by the hMOB1 Protein

Contact Info

Product

Resources

About