scholarly journals Diversity, classification and function of the plant protein kinase superfamily

2012 ◽  
Vol 367 (1602) ◽  
pp. 2619-2639 ◽  
Author(s):  
Melissa D. Lehti-Shiu ◽  
Shin-Han Shiu
Keyword(s):  
Protein Kinase ◽  
Protein Kinases ◽  
Plant Protein ◽  
Flowering Plant ◽  
Cellular Functions ◽  
Functional Protein ◽  
Low Copy Number ◽  
Receptor Like Kinase ◽  
Insufficient Time ◽  
And Function

Eukaryotic protein kinases belong to a large superfamily with hundreds to thousands of copies and are components of essentially all cellular functions. The goals of this study are to classify protein kinases from 25 plant species and to assess their evolutionary history in conjunction with consideration of their molecular functions. The protein kinase superfamily has expanded in the flowering plant lineage, in part through recent duplications. As a result, the flowering plant protein kinase repertoire, or kinome, is in general significantly larger than other eukaryotes, ranging in size from 600 to 2500 members. This large variation in kinome size is mainly due to the expansion and contraction of a few families, particularly the receptor-like kinase/Pelle family. A number of protein kinases reside in highly conserved, low copy number families and often play broadly conserved regulatory roles in metabolism and cell division, although functions of plant homologues have often diverged from their metazoan counterparts. Members of expanded plant kinase families often have roles in plant-specific processes and some may have contributed to adaptive evolution. Nonetheless, non-adaptive explanations, such as kinase duplicate subfunctionalization and insufficient time for pseudogenization, may also contribute to the large number of seemingly functional protein kinases in plants.

scholarly journals Classification of Nonenzymatic Homologues of Protein Kinases

2009 ◽  
Vol 2009 ◽  
pp. 1-17 ◽  
Author(s):  
K. Anamika ◽  
K. R. Abhinandan ◽  
K. Deshmukh ◽  
N. Srinivasan
Keyword(s):  
Protein Kinase ◽  
Protein Kinases ◽  
Protein Interaction ◽  
Transmembrane Domain ◽  
Homo Sapiens ◽  
Interaction Domain ◽  
Protein Protein Interaction ◽  
Domain 3 ◽  
Eukaryotic Organisms ◽  
And Function

Protein Kinase-Like Non-kinases (PKLNKs), which are closely related to protein kinases, lack the crucial catalytic aspartate in the catalytic loop, and hence cannot function as protein kinase, have been analysed. Using various sensitive sequence analysis methods, we have recognized 82 PKLNKs from four higher eukaryotic organisms, namely,Homo sapiens,Mus musculus,Rattus norvegicus, andDrosophila melanogaster. On the basis of their domain combination and function, PKLNKs have been classified mainly into four categories: (1) Ligand binding PKLNKs, (2) PKLNKs with extracellular protein-protein interaction domain, (3) PKLNKs involved in dimerization, and (4) PKLNKs with cytoplasmic protein-protein interaction module. While members of the first two classes of PKLNKs have transmembrane domain tethered to the PKLNK domain, members of the other two classes of PKLNKs are cytoplasmic in nature. The current classification scheme hopes to provide a convenient framework to classify the PKLNKs from other eukaryotes which would be helpful in deciphering their roles in cellular processes.

scholarly journals Homeodomain-interacting protein kinase (Hipk) is required for nervous system and muscle structure and function

2019 ◽  
Author(s):  
Simon Wang ◽  
Donald A.R. Sinclair ◽  
Hae-Yoon Kim ◽  
Stephen D. Kinsey ◽  
Byoungjoo Yoo ◽  
...  
Keyword(s):  
Nervous System ◽  
Protein Kinase ◽  
Motor Neuron ◽  
Protein Kinases ◽  
Genetic Manipulation ◽  
Motor Neuron Diseases ◽  
Muscle Involvement ◽  
Interacting Protein ◽  
Larval Neuromuscular Junction ◽  
And Function

AbstractHomeodomain-interacting protein kinases (Hipk) have been previously associated with cell proliferation and cancer, however, their effects in the nervous system are less well understood. We have used Drosophila melanogaster to evaluate the effects of altered Hipk expression on the nervous system and muscle. Using genetic manipulation of Hipk expression we demonstrate that knockdown and over-expression of Hipk produces early adult lethality, partially due to the effects on the nervous system and muscle involvement. We find that optimal levels of Hipk are critical for the function of dopaminergic neurons and glial cells in the nervous system, as well as muscle. Furthermore, manipulation of Hipk affects the structure of the larval neuromuscular junction (NMJ) and increases motor neuron axonal branching. Hipk regulates the phosphorylation of the synapse-associated cytoskeletal protein Hts (adducin) and modulates the expression of two important protein kinases, Calcium-calmodulin protein kinase II (CaMKII) and Partitioning-defective 1 (PAR-1), all of which may alter neuromuscular function and influence lethality. Hipk also modifies the distribution of an important nuclear protein, TBPH, the fly orthologue of TAR DNA-binding protein 43 (TDP-43), which may have relevance for understanding motor neuron diseases.

scholarly journals Functions and regulation of the serine/threonine protein kinase CK1 family: moving beyond promiscuity

2020 ◽  
Vol 477 (23) ◽  
pp. 4603-4621
Author(s):  
Luke J. Fulcher ◽  
Gopal P. Sapkota
Keyword(s):  
Protein Kinase ◽  
Protein Kinases ◽  
Therapeutic Targets ◽  
Signalling Pathways ◽  
Biological Processes ◽  
Cellular Functions ◽  
Intracellular Regulation ◽  
Constitutively Active

Regarded as constitutively active enzymes, known to participate in many, diverse biological processes, the intracellular regulation bestowed on the CK1 family of serine/threonine protein kinases is critically important, yet poorly understood. Here, we provide an overview of the known CK1-dependent cellular functions and review the emerging roles of CK1-regulating proteins in these processes. We go on to discuss the advances, limitations and pitfalls that CK1 researchers encounter when attempting to define relationships between CK1 isoforms and their substrates, and the challenges associated with ascertaining the correct physiological CK1 isoform for the substrate of interest. With increasing interest in CK1 isoforms as therapeutic targets, methods of selectively inhibiting CK1 isoform-specific processes is warranted, yet challenging to achieve given their participation in such a vast plethora of signalling pathways. Here, we discuss how one might shut down CK1-specific processes, without impacting other aspects of CK1 biology.

Structure and function of MK5/PRAK: the loner among the mitogen-activated protein kinase-activated protein kinases

2013 ◽  
Vol 394 (9) ◽  
pp. 1115-1132 ◽  
Author(s):  
Ugo Moens ◽  
Sergiy Kostenko
Keyword(s):  
Protein Kinase ◽  
Protein Kinases ◽  
Kinase Domain ◽  
Mitogen Activated Protein Kinase ◽  
Cellular Processes ◽  
Mapk Pathways ◽  
Mitogen Activated Protein ◽  
Kinase Cascade ◽  
Apoptosis Gene ◽  
And Function

Abstract Mitogen-activated protein kinase (MAPK) pathways are important signal transduction pathways that control pivotal cellular processes including proliferation, differentiation, survival, apoptosis, gene regulation, and motility. MAPK pathways consist of a relay of consecutive phosphorylation events exerted by MAPK kinase kinases, MAPK kinases, and MAPKs. Conventional MAPKs are characterized by a conserved Thr-X-Tyr motif in the activation loop of the kinase domain, while atypical MAPKs lack this motif and do not seem to be organized into the classical three-tiered kinase cascade. One functional group of conventional and atypical MAPK substrates consists of protein kinases known as MAPK-activated protein kinases. Eleven mammalian MAPK-activated protein kinases have been identified, and they are divided into five subgroups: the ribosomal-S6-kinases RSK1-4, the MAPK-interacting kinases MNK1 and 2, the mitogen- and stress-activated kinases MSK1 and 2, the MAPK-activated protein kinases MK2 and 3, and the MAPK-activated protein kinase MK5 (also referred to as PRAK). MK5/PRAK is the only MAPK-activated protein kinase that is a substrate for both conventional and atypical MAPK, while all other MAPKAPKs are exclusively phosphorylated by conventional MAPKs. This review focuses on the structure, activation, substrates, functions, and possible implications of MK5/PRAK in malignant and nonmalignant diseases.

scholarly journals Kinase-interacting substrate screening is a novel method to identify kinase substrates

2015 ◽  
Vol 209 (6) ◽  
pp. 895-912 ◽  
Author(s):  
Mutsuki Amano ◽  
Tomonari Hamaguchi ◽  
Md. Hasanuzzaman Shohag ◽  
Kei Kozawa ◽  
Katsuhiro Kato ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinases ◽  
Ternary Complex ◽  
Rho Kinase ◽  
Phosphorylation Sites ◽  
Dependent Manner ◽  
Cellular Functions ◽  
Associated Proteins ◽  
Novel Method ◽  
Kinase Substrates

Protein kinases play pivotal roles in numerous cellular functions; however, the specific substrates of each protein kinase have not been fully elucidated. We have developed a novel method called kinase-interacting substrate screening (KISS). Using this method, 356 phosphorylation sites of 140 proteins were identified as candidate substrates for Rho-associated kinase (Rho-kinase/ROCK2), including known substrates. The KISS method was also applied to additional kinases, including PKA, MAPK1, CDK5, CaMK1, PAK7, PKN, LYN, and FYN, and a lot of candidate substrates and their phosphorylation sites were determined, most of which have not been reported previously. Among the candidate substrates for Rho-kinase, several functional clusters were identified, including the polarity-associated proteins, such as Scrib. We found that Scrib plays a crucial role in the regulation of subcellular contractility by assembling into a ternary complex with Rho-kinase and Shroom2 in a phosphorylation-dependent manner. We propose that the KISS method is a comprehensive and useful substrate screen for various kinases.

Who does TORC2 talk to?

2018 ◽  
Vol 475 (10) ◽  
pp. 1721-1738 ◽  
Author(s):  
Jianling Xie ◽  
Xuemin Wang ◽  
Christopher G. Proud
Keyword(s):  
Protein Kinase ◽  
Protein Kinases ◽  
Gene Transcription ◽  
Cell Metabolism ◽  
Cellular Functions ◽  
Cellular Physiology ◽  
Cell Functions ◽  
Wide Range ◽  
And Control ◽  
Partner Proteins

The target of rapamycin (TOR) is a protein kinase that, by forming complexes with partner proteins, governs diverse cellular signalling networks to regulate a wide range of processes. TOR thus plays central roles in maintaining normal cellular functions and, when dysregulated, in diverse diseases. TOR forms two distinct types of multiprotein complexes (TOR complexes 1 and 2, TORC1 and TORC2). TORC1 and TORC2 differ in their composition, their control and their substrates, so that they play quite distinct roles in cellular physiology. Much effort has been focused on deciphering the detailed regulatory links within the TOR pathways and the structure and control of TOR complexes. In this review, we summarize recent advances in understanding mammalian (m) TORC2, its structure, its regulation, and its substrates, which link TORC2 signalling to the control of cell functions. It is now clear that TORC2 regulates several aspects of cell metabolism, including lipogenesis and glucose transport. It also regulates gene transcription, the cytoskeleton, and the activity of a subset of other protein kinases.

Spatial control of actin-based motility through plasmalemmal PtdIns(4,5)P2-rich raft assemblies.

2005 ◽  
Vol 72 ◽  
pp. 119-127 ◽  
Author(s):  
Tamara Golub ◽  
Caroni Pico
Keyword(s):  
Protein Kinase ◽  
Cell Surface ◽  
Actin Cytoskeleton ◽  
Lipid Rafts ◽  
Patch Clustering ◽  
Pkc Protein Kinase C ◽  
Membrane Bound ◽  
And Function ◽  
Cytoskeleton Dynamics ◽  
Syndrome Protein

The interactions of cells with their environment involve regulated actin-based motility at defined positions along the cell surface. Sphingolipid- and cholesterol-dependent microdomains (rafts) order proteins at biological membranes, and have been implicated in most signalling processes at the cell surface. Many membrane-bound components that regulate actin cytoskeleton dynamics and cell-surface motility associate with PtdIns(4,5)P2-rich lipid rafts. Although raft integrity is not required for substrate-directed cell spreading, or to initiate signalling for motility, it is a prerequisite for sustained and organized motility. Plasmalemmal rafts redistribute rapidly in response to signals, triggering motility. This process involves the removal of rafts from sites that are not interacting with the substrate, apparently through endocytosis, and a local accumulation at sites of integrin-mediated substrate interactions. PtdIns(4,5)P2-rich lipid rafts can assemble into patches in a process depending on PtdIns(4,5)P2, Cdc42 (cell-division control 42), N-WASP (neural Wiskott-Aldrich syndrome protein) and actin cytoskeleton dynamics. The raft patches are sites of signal-induced actin assembly, and their accumulation locally promotes sustained motility. The patches capture microtubules, which promote patch clustering through PKA (protein kinase A), to steer motility. Raft accumulation at the cell surface, and its coupling to motility are influenced greatly by the expression of intrinsic raft-associated components that associate with the cytosolic leaflet of lipid rafts. Among them, GAP43 (growth-associated protein 43)-like proteins interact with PtdIns(4,5)P2 in a Ca2+/calmodulin and PKC (protein kinase C)-regulated manner, and function as intrinsic determinants of motility and anatomical plasticity. Plasmalemmal PtdIns(4,5)P2-rich raft assemblies thus provide powerful organizational principles for tight spatial and temporal control of signalling in motility.

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